The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana
Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate‐biosynthetic pathway leading to S‐lysine: the decarboxylation of meso‐diaminopimelate to form S‐lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of...
Gespeichert in:
| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-05, Vol.70 (5), p.663-668 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 668 |
|---|---|
| container_issue | 5 |
| container_start_page | 663 |
| container_title | Acta crystallographica. Section F, Structural biology communications |
| container_volume | 70 |
| creator | Oliver, Michael R. Crowther, Jennifer M. Leeman, Mary M. Kessans, Sarah A. North, Rachel A. Donovan, Katherine A. Griffin, Michael D. W. Suzuki, Hironori Hudson, André O. Kasanmascheff, Müge Dobson, Renwick C. J. |
| description | Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate‐biosynthetic pathway leading to S‐lysine: the decarboxylation of meso‐diaminopimelate to form S‐lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of animals. Thus, the diaminopimelate pathway represents an attractive target for antimicrobial and herbicide treatments and has received considerable attention from both a mechanistic and a structural viewpoint. Diaminopimelate decarboxylase has only been characterized in prokaryotic species. This communication describes the first structural studies of two diaminopimelate decarboxylase isoforms from a plant. The Arabidopsis thaliana diaminopimelate decarboxylase cDNAs At3g14390 (encoding DapDc1) and At5g11880 (encoding DapDc2) were cloned from genomic DNA and the recombinant proteins were expressed and purified from Escherichia coli Rosetta (DE3) cells. The crystals of DapDc1 and DapDc2 diffracted to beyond 2.00 and 2.27 Å resolution, respectively. Understanding the structural biology of diaminopimelate decarboxylase from a eukaryotic species will provide insights for the development of future herbicide treatments, in particular. |
| doi_str_mv | 10.1107/S2053230X14007699 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4014342</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1524168874</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4720-558c24de95196f572b250eaed3c87699142ecc310240e4e4e2891d838de044af3</originalsourceid><addsrcrecordid>eNqFkctu1DAUhiMEolXpA7BBltiwIMXXcbJBGo1oC4zKgiLKyvI4J4yLEwc7oQ3P0ofFmRlGBRbIC_scf_-vc8mypwSfEILlq48UC0YZviIcYzkrywfZ4ZTKp9zDe--D7DjGa4zxJCOyfJwdUF4QKRk7zO4u14C6IdjaGt1b375EJoyx187Zn5sE0m2FugDONrbVYURXedAjqmxdB212hHZjtBH5GvU3Htnoax-aTdxA9HlldRL7zjbgdA-oAqPDyt-OTkdAdfANmge9spXvJpt-rZ1Npk-yR7V2EY5391H26fTN5eI8X344e7uYL3PDJcW5EIWhvIJSkHJWC0lXVGDQUDFTTIMhnIIxjGDKMfB0aFGSqmBFBZhzXbOj7PXWtxtWDVQG2j5op7pgm9Sw8tqqP39au1Zf_Q_FMeGM02TwYmcQ_PcBYq8aGw04p1vwQ1REUE5mRSF5Qp__hV77IaQBbihKRSq5SBTZUib4GAPU-2IIVtMe1T_rT5pn97vYK34vOwHlFrixDsb_O6r5l1N6vhBE4qTNt1obe7jda3X4pmaSSaE-X5ypd_y9LJYXQkn2C0dBzhM</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1522258768</pqid></control><display><type>article</type><title>The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana</title><source>Wiley Online Library - AutoHoldings Journals</source><source>MEDLINE</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Oliver, Michael R. ; Crowther, Jennifer M. ; Leeman, Mary M. ; Kessans, Sarah A. ; North, Rachel A. ; Donovan, Katherine A. ; Griffin, Michael D. W. ; Suzuki, Hironori ; Hudson, André O. ; Kasanmascheff, Müge ; Dobson, Renwick C. J.</creator><creatorcontrib>Oliver, Michael R. ; Crowther, Jennifer M. ; Leeman, Mary M. ; Kessans, Sarah A. ; North, Rachel A. ; Donovan, Katherine A. ; Griffin, Michael D. W. ; Suzuki, Hironori ; Hudson, André O. ; Kasanmascheff, Müge ; Dobson, Renwick C. J.</creatorcontrib><description>Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate‐biosynthetic pathway leading to S‐lysine: the decarboxylation of meso‐diaminopimelate to form S‐lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of animals. Thus, the diaminopimelate pathway represents an attractive target for antimicrobial and herbicide treatments and has received considerable attention from both a mechanistic and a structural viewpoint. Diaminopimelate decarboxylase has only been characterized in prokaryotic species. This communication describes the first structural studies of two diaminopimelate decarboxylase isoforms from a plant. The Arabidopsis thaliana diaminopimelate decarboxylase cDNAs At3g14390 (encoding DapDc1) and At5g11880 (encoding DapDc2) were cloned from genomic DNA and the recombinant proteins were expressed and purified from Escherichia coli Rosetta (DE3) cells. The crystals of DapDc1 and DapDc2 diffracted to beyond 2.00 and 2.27 Å resolution, respectively. Understanding the structural biology of diaminopimelate decarboxylase from a eukaryotic species will provide insights for the development of future herbicide treatments, in particular.</description><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X14007699</identifier><identifier>PMID: 24817733</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; antibiotic resistance ; antibiotics ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Carboxy-Lyases - chemistry ; Carboxy-Lyases - genetics ; Carboxy-Lyases - isolation & purification ; Crystallization ; Crystallization Communications ; diaminopimelate ; diaminopimelate decarboxylase ; drug discovery ; herbicides ; Isoenzymes - chemistry ; Isoenzymes - genetics ; Isoenzymes - isolation & purification ; lysine biosynthesis ; Molecular Sequence Data ; S-lysine ; X-Ray Diffraction</subject><ispartof>Acta crystallographica. Section F, Structural biology communications, 2014-05, Vol.70 (5), p.663-668</ispartof><rights>International Union of Crystallography, 2014</rights><rights>International Union of Crystallography 2014 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4720-558c24de95196f572b250eaed3c87699142ecc310240e4e4e2891d838de044af3</citedby><cites>FETCH-LOGICAL-c4720-558c24de95196f572b250eaed3c87699142ecc310240e4e4e2891d838de044af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014342/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4014342/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,729,782,786,887,1419,27931,27932,45581,45582,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24817733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oliver, Michael R.</creatorcontrib><creatorcontrib>Crowther, Jennifer M.</creatorcontrib><creatorcontrib>Leeman, Mary M.</creatorcontrib><creatorcontrib>Kessans, Sarah A.</creatorcontrib><creatorcontrib>North, Rachel A.</creatorcontrib><creatorcontrib>Donovan, Katherine A.</creatorcontrib><creatorcontrib>Griffin, Michael D. W.</creatorcontrib><creatorcontrib>Suzuki, Hironori</creatorcontrib><creatorcontrib>Hudson, André O.</creatorcontrib><creatorcontrib>Kasanmascheff, Müge</creatorcontrib><creatorcontrib>Dobson, Renwick C. J.</creatorcontrib><title>The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana</title><title>Acta crystallographica. Section F, Structural biology communications</title><addtitle>Acta Crystallographica Section F</addtitle><description>Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate‐biosynthetic pathway leading to S‐lysine: the decarboxylation of meso‐diaminopimelate to form S‐lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of animals. Thus, the diaminopimelate pathway represents an attractive target for antimicrobial and herbicide treatments and has received considerable attention from both a mechanistic and a structural viewpoint. Diaminopimelate decarboxylase has only been characterized in prokaryotic species. This communication describes the first structural studies of two diaminopimelate decarboxylase isoforms from a plant. The Arabidopsis thaliana diaminopimelate decarboxylase cDNAs At3g14390 (encoding DapDc1) and At5g11880 (encoding DapDc2) were cloned from genomic DNA and the recombinant proteins were expressed and purified from Escherichia coli Rosetta (DE3) cells. The crystals of DapDc1 and DapDc2 diffracted to beyond 2.00 and 2.27 Å resolution, respectively. Understanding the structural biology of diaminopimelate decarboxylase from a eukaryotic species will provide insights for the development of future herbicide treatments, in particular.</description><subject>Amino Acid Sequence</subject><subject>antibiotic resistance</subject><subject>antibiotics</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Carboxy-Lyases - chemistry</subject><subject>Carboxy-Lyases - genetics</subject><subject>Carboxy-Lyases - isolation & purification</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>diaminopimelate</subject><subject>diaminopimelate decarboxylase</subject><subject>drug discovery</subject><subject>herbicides</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - isolation & purification</subject><subject>lysine biosynthesis</subject><subject>Molecular Sequence Data</subject><subject>S-lysine</subject><subject>X-Ray Diffraction</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctu1DAUhiMEolXpA7BBltiwIMXXcbJBGo1oC4zKgiLKyvI4J4yLEwc7oQ3P0ofFmRlGBRbIC_scf_-vc8mypwSfEILlq48UC0YZviIcYzkrywfZ4ZTKp9zDe--D7DjGa4zxJCOyfJwdUF4QKRk7zO4u14C6IdjaGt1b375EJoyx187Zn5sE0m2FugDONrbVYURXedAjqmxdB212hHZjtBH5GvU3Htnoax-aTdxA9HlldRL7zjbgdA-oAqPDyt-OTkdAdfANmge9spXvJpt-rZ1Npk-yR7V2EY5391H26fTN5eI8X344e7uYL3PDJcW5EIWhvIJSkHJWC0lXVGDQUDFTTIMhnIIxjGDKMfB0aFGSqmBFBZhzXbOj7PXWtxtWDVQG2j5op7pgm9Sw8tqqP39au1Zf_Q_FMeGM02TwYmcQ_PcBYq8aGw04p1vwQ1REUE5mRSF5Qp__hV77IaQBbihKRSq5SBTZUib4GAPU-2IIVtMe1T_rT5pn97vYK34vOwHlFrixDsb_O6r5l1N6vhBE4qTNt1obe7jda3X4pmaSSaE-X5ypd_y9LJYXQkn2C0dBzhM</recordid><startdate>201405</startdate><enddate>201405</enddate><creator>Oliver, Michael R.</creator><creator>Crowther, Jennifer M.</creator><creator>Leeman, Mary M.</creator><creator>Kessans, Sarah A.</creator><creator>North, Rachel A.</creator><creator>Donovan, Katherine A.</creator><creator>Griffin, Michael D. W.</creator><creator>Suzuki, Hironori</creator><creator>Hudson, André O.</creator><creator>Kasanmascheff, Müge</creator><creator>Dobson, Renwick C. J.</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201405</creationdate><title>The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana</title><author>Oliver, Michael R. ; Crowther, Jennifer M. ; Leeman, Mary M. ; Kessans, Sarah A. ; North, Rachel A. ; Donovan, Katherine A. ; Griffin, Michael D. W. ; Suzuki, Hironori ; Hudson, André O. ; Kasanmascheff, Müge ; Dobson, Renwick C. J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4720-558c24de95196f572b250eaed3c87699142ecc310240e4e4e2891d838de044af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>antibiotic resistance</topic><topic>antibiotics</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Carboxy-Lyases - chemistry</topic><topic>Carboxy-Lyases - genetics</topic><topic>Carboxy-Lyases - isolation & purification</topic><topic>Crystallization</topic><topic>Crystallization Communications</topic><topic>diaminopimelate</topic><topic>diaminopimelate decarboxylase</topic><topic>drug discovery</topic><topic>herbicides</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - isolation & purification</topic><topic>lysine biosynthesis</topic><topic>Molecular Sequence Data</topic><topic>S-lysine</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oliver, Michael R.</creatorcontrib><creatorcontrib>Crowther, Jennifer M.</creatorcontrib><creatorcontrib>Leeman, Mary M.</creatorcontrib><creatorcontrib>Kessans, Sarah A.</creatorcontrib><creatorcontrib>North, Rachel A.</creatorcontrib><creatorcontrib>Donovan, Katherine A.</creatorcontrib><creatorcontrib>Griffin, Michael D. W.</creatorcontrib><creatorcontrib>Suzuki, Hironori</creatorcontrib><creatorcontrib>Hudson, André O.</creatorcontrib><creatorcontrib>Kasanmascheff, Müge</creatorcontrib><creatorcontrib>Dobson, Renwick C. J.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oliver, Michael R.</au><au>Crowther, Jennifer M.</au><au>Leeman, Mary M.</au><au>Kessans, Sarah A.</au><au>North, Rachel A.</au><au>Donovan, Katherine A.</au><au>Griffin, Michael D. W.</au><au>Suzuki, Hironori</au><au>Hudson, André O.</au><au>Kasanmascheff, Müge</au><au>Dobson, Renwick C. J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana</atitle><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle><addtitle>Acta Crystallographica Section F</addtitle><date>2014-05</date><risdate>2014</risdate><volume>70</volume><issue>5</issue><spage>663</spage><epage>668</epage><pages>663-668</pages><issn>2053-230X</issn><eissn>2053-230X</eissn><abstract>Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate‐biosynthetic pathway leading to S‐lysine: the decarboxylation of meso‐diaminopimelate to form S‐lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of animals. Thus, the diaminopimelate pathway represents an attractive target for antimicrobial and herbicide treatments and has received considerable attention from both a mechanistic and a structural viewpoint. Diaminopimelate decarboxylase has only been characterized in prokaryotic species. This communication describes the first structural studies of two diaminopimelate decarboxylase isoforms from a plant. The Arabidopsis thaliana diaminopimelate decarboxylase cDNAs At3g14390 (encoding DapDc1) and At5g11880 (encoding DapDc2) were cloned from genomic DNA and the recombinant proteins were expressed and purified from Escherichia coli Rosetta (DE3) cells. The crystals of DapDc1 and DapDc2 diffracted to beyond 2.00 and 2.27 Å resolution, respectively. Understanding the structural biology of diaminopimelate decarboxylase from a eukaryotic species will provide insights for the development of future herbicide treatments, in particular.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>24817733</pmid><doi>10.1107/S2053230X14007699</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2053-230X |
| ispartof | Acta crystallographica. Section F, Structural biology communications, 2014-05, Vol.70 (5), p.663-668 |
| issn | 2053-230X 2053-230X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4014342 |
| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence antibiotic resistance antibiotics Arabidopsis - enzymology Arabidopsis - genetics Carboxy-Lyases - chemistry Carboxy-Lyases - genetics Carboxy-Lyases - isolation & purification Crystallization Crystallization Communications diaminopimelate diaminopimelate decarboxylase drug discovery herbicides Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - isolation & purification lysine biosynthesis Molecular Sequence Data S-lysine X-Ray Diffraction |
| title | The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-04T13%3A59%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20purification,%20crystallization%20and%20preliminary%20X-ray%20diffraction%20analysis%20of%20two%20isoforms%20of%20meso-diaminopimelate%20decarboxylase%20from%20Arabidopsis%20thaliana&rft.jtitle=Acta%20crystallographica.%20Section%20F,%20Structural%20biology%20communications&rft.au=Oliver,%20Michael%20R.&rft.date=2014-05&rft.volume=70&rft.issue=5&rft.spage=663&rft.epage=668&rft.pages=663-668&rft.issn=2053-230X&rft.eissn=2053-230X&rft_id=info:doi/10.1107/S2053230X14007699&rft_dat=%3Cproquest_pubme%3E1524168874%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1522258768&rft_id=info:pmid/24817733&rfr_iscdi=true |