Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum
The malic enzyme from muscle mitochondria of the parasitic nematode Ascaris suum is a tetramer of 65 kDa monomers that catalyzes the oxidative decarboxylation of malate to pyruvate and CO 2 with NAD cofactor as oxidant. This malic enzyme is critical to the nematode for muscle function under anaerobi...
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| Veröffentlicht in: | Journal of molecular biology 1992-07, Vol.226 (2), p.565-569 |
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| creator | Clancy, L.L. Rao, G.S.J. Finzel, B.C. Muchmore, S.W. Holland, D.R. Watenpaugh, K.D. Krishnamurthy, H.M. Sweet, R.M. Cook, P.F. Harris, B.G. Einspahr, H.M. |
| description | The malic enzyme from muscle mitochondria of the parasitic nematode
Ascaris suum is a tetramer of 65 kDa monomers that catalyzes the oxidative decarboxylation of malate to pyruvate and CO
2 with NAD cofactor as oxidant. This malic enzyme is critical to the nematode for muscle function under anaerobic conditions. Unlike mammalian versions of the enzyme such as that found in rat liver, which require NADP as cofactor, the nematode version is an NAD-dependent enzyme. We report the crystallization of samples of the nematode enzyme at room temperature from pH 7.5 solutions of polyethylene glycol 4000 containing magnesium sulfate, NAD and sodium tartronate. Immediately upon mixing of protein and precipitant solutions, a marked precipitation of the protein occurs. Out of this precipitate, crystals appear almost immediately, most commonly in a truncated cube form that can grow to 0.5 to 0.7 mm on a cube edge in two to three days. The crystals are trigonal, space group
P3
1
21 or its enantiomer, with
a = b = 131.2(7)
A
̊
, c = 152.6(9)
A
̊
, and two monomers per asymmetric unit. Fresh crystals diffract X-radiation from a synchrotron source (λ = 0.95 Å) to about 3.0 Å resolution. Rotational analysis of Patterson functions indicates that the malic enzyme tetramer has 222 symmetry. |
| doi_str_mv | 10.1016/0022-2836(92)90971-L |
| format | Article |
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Ascaris suum is a tetramer of 65 kDa monomers that catalyzes the oxidative decarboxylation of malate to pyruvate and CO
2 with NAD cofactor as oxidant. This malic enzyme is critical to the nematode for muscle function under anaerobic conditions. Unlike mammalian versions of the enzyme such as that found in rat liver, which require NADP as cofactor, the nematode version is an NAD-dependent enzyme. We report the crystallization of samples of the nematode enzyme at room temperature from pH 7.5 solutions of polyethylene glycol 4000 containing magnesium sulfate, NAD and sodium tartronate. Immediately upon mixing of protein and precipitant solutions, a marked precipitation of the protein occurs. Out of this precipitate, crystals appear almost immediately, most commonly in a truncated cube form that can grow to 0.5 to 0.7 mm on a cube edge in two to three days. The crystals are trigonal, space group
P3
1
21 or its enantiomer, with
a = b = 131.2(7)
A
̊
, c = 152.6(9)
A
̊
, and two monomers per asymmetric unit. Fresh crystals diffract X-radiation from a synchrotron source (λ = 0.95 Å) to about 3.0 Å resolution. Rotational analysis of Patterson functions indicates that the malic enzyme tetramer has 222 symmetry.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(92)90971-L</identifier><identifier>PMID: 1640469</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Animals ; Ascaris - enzymology ; Ascaris suum ; Biological and medical sciences ; crystal structure ; Crystalline structure ; crystallization ; Crystallography ; Fundamental and applied biological sciences. Psychology ; malate dehydrogenase (oxaloacetate-decarboxylating) ; Malate Dehydrogenase - chemistry ; Malate Dehydrogenase - ultrastructure ; malic enzyme ; Mitochondria - enzymology ; Molecular biophysics ; molecular conformation ; NAD-dependent ; parasitic nematode ; Protein Conformation ; Structure in molecular biology ; X-ray diffraction</subject><ispartof>Journal of molecular biology, 1992-07, Vol.226 (2), p.565-569</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-d3900cfa90f21ad36d8f1bc209a547580fd3d9925526cdc4f3ca676dea82db7a3</citedby><cites>FETCH-LOGICAL-c441t-d3900cfa90f21ad36d8f1bc209a547580fd3d9925526cdc4f3ca676dea82db7a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(92)90971-L$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5461826$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1640469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clancy, L.L.</creatorcontrib><creatorcontrib>Rao, G.S.J.</creatorcontrib><creatorcontrib>Finzel, B.C.</creatorcontrib><creatorcontrib>Muchmore, S.W.</creatorcontrib><creatorcontrib>Holland, D.R.</creatorcontrib><creatorcontrib>Watenpaugh, K.D.</creatorcontrib><creatorcontrib>Krishnamurthy, H.M.</creatorcontrib><creatorcontrib>Sweet, R.M.</creatorcontrib><creatorcontrib>Cook, P.F.</creatorcontrib><creatorcontrib>Harris, B.G.</creatorcontrib><creatorcontrib>Einspahr, H.M.</creatorcontrib><title>Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The malic enzyme from muscle mitochondria of the parasitic nematode
Ascaris suum is a tetramer of 65 kDa monomers that catalyzes the oxidative decarboxylation of malate to pyruvate and CO
2 with NAD cofactor as oxidant. This malic enzyme is critical to the nematode for muscle function under anaerobic conditions. Unlike mammalian versions of the enzyme such as that found in rat liver, which require NADP as cofactor, the nematode version is an NAD-dependent enzyme. We report the crystallization of samples of the nematode enzyme at room temperature from pH 7.5 solutions of polyethylene glycol 4000 containing magnesium sulfate, NAD and sodium tartronate. Immediately upon mixing of protein and precipitant solutions, a marked precipitation of the protein occurs. Out of this precipitate, crystals appear almost immediately, most commonly in a truncated cube form that can grow to 0.5 to 0.7 mm on a cube edge in two to three days. The crystals are trigonal, space group
P3
1
21 or its enantiomer, with
a = b = 131.2(7)
A
̊
, c = 152.6(9)
A
̊
, and two monomers per asymmetric unit. Fresh crystals diffract X-radiation from a synchrotron source (λ = 0.95 Å) to about 3.0 Å resolution. Rotational analysis of Patterson functions indicates that the malic enzyme tetramer has 222 symmetry.</description><subject>Animals</subject><subject>Ascaris - enzymology</subject><subject>Ascaris suum</subject><subject>Biological and medical sciences</subject><subject>crystal structure</subject><subject>Crystalline structure</subject><subject>crystallization</subject><subject>Crystallography</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>malate dehydrogenase (oxaloacetate-decarboxylating)</subject><subject>Malate Dehydrogenase - chemistry</subject><subject>Malate Dehydrogenase - ultrastructure</subject><subject>malic enzyme</subject><subject>Mitochondria - enzymology</subject><subject>Molecular biophysics</subject><subject>molecular conformation</subject><subject>NAD-dependent</subject><subject>parasitic nematode</subject><subject>Protein Conformation</subject><subject>Structure in molecular biology</subject><subject>X-ray diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1v1DAQgGELgcq28A9A5IAQHAL-TnxBWm35klZwgF64WLP2GIySeGsnSNtfT7ZZlRucfJhnRtZLyBNGXzPK9BtKOa95K_RLw18ZahpWb--RFaOtqVst2vtkdUcekvNSflFKlZDtGTljWlKpzYp83-RDGaHr4g2MMQ1VCtX4E6vP68va4x4Hj8NY9dBFV-Fwc-ixCjn1t2YPGUoc58mAPYzJY7UuDnIsVZmm_hF5EKAr-Pj0XpCr9---bT7W2y8fPm3W29pJycbaC0OpC2Bo4Ay80L4NbOc4NaBko1oavPDGcKW4dt7JIBzoRnuElvtdA-KCvFju7nO6nrCMto_FYdfBgGkqthFsziDFfyHTQimmjlAu0OVUSsZg9zn2kA-WUXtsb49h7TGsNdzetrfbee3p6f6069H_XVpiz_PnpznMmbqQYXCx3DElNWu5ntmzhQVIFn7MOe3VV06ZoKxRhgk-i7eLwDnr74jZFhdxcOhjRjdan-K_f_oHX8upaQ</recordid><startdate>19920720</startdate><enddate>19920720</enddate><creator>Clancy, L.L.</creator><creator>Rao, G.S.J.</creator><creator>Finzel, B.C.</creator><creator>Muchmore, S.W.</creator><creator>Holland, D.R.</creator><creator>Watenpaugh, K.D.</creator><creator>Krishnamurthy, H.M.</creator><creator>Sweet, R.M.</creator><creator>Cook, P.F.</creator><creator>Harris, B.G.</creator><creator>Einspahr, H.M.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920720</creationdate><title>Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum</title><author>Clancy, L.L. ; Rao, G.S.J. ; Finzel, B.C. ; Muchmore, S.W. ; Holland, D.R. ; Watenpaugh, K.D. ; Krishnamurthy, H.M. ; Sweet, R.M. ; Cook, P.F. ; Harris, B.G. ; Einspahr, H.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-d3900cfa90f21ad36d8f1bc209a547580fd3d9925526cdc4f3ca676dea82db7a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Ascaris - enzymology</topic><topic>Ascaris suum</topic><topic>Biological and medical sciences</topic><topic>crystal structure</topic><topic>Crystalline structure</topic><topic>crystallization</topic><topic>Crystallography</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>malate dehydrogenase (oxaloacetate-decarboxylating)</topic><topic>Malate Dehydrogenase - chemistry</topic><topic>Malate Dehydrogenase - ultrastructure</topic><topic>malic enzyme</topic><topic>Mitochondria - enzymology</topic><topic>Molecular biophysics</topic><topic>molecular conformation</topic><topic>NAD-dependent</topic><topic>parasitic nematode</topic><topic>Protein Conformation</topic><topic>Structure in molecular biology</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Clancy, L.L.</creatorcontrib><creatorcontrib>Rao, G.S.J.</creatorcontrib><creatorcontrib>Finzel, B.C.</creatorcontrib><creatorcontrib>Muchmore, S.W.</creatorcontrib><creatorcontrib>Holland, D.R.</creatorcontrib><creatorcontrib>Watenpaugh, K.D.</creatorcontrib><creatorcontrib>Krishnamurthy, H.M.</creatorcontrib><creatorcontrib>Sweet, R.M.</creatorcontrib><creatorcontrib>Cook, P.F.</creatorcontrib><creatorcontrib>Harris, B.G.</creatorcontrib><creatorcontrib>Einspahr, H.M.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Clancy, L.L.</au><au>Rao, G.S.J.</au><au>Finzel, B.C.</au><au>Muchmore, S.W.</au><au>Holland, D.R.</au><au>Watenpaugh, K.D.</au><au>Krishnamurthy, H.M.</au><au>Sweet, R.M.</au><au>Cook, P.F.</au><au>Harris, B.G.</au><au>Einspahr, H.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1992-07-20</date><risdate>1992</risdate><volume>226</volume><issue>2</issue><spage>565</spage><epage>569</epage><pages>565-569</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The malic enzyme from muscle mitochondria of the parasitic nematode
Ascaris suum is a tetramer of 65 kDa monomers that catalyzes the oxidative decarboxylation of malate to pyruvate and CO
2 with NAD cofactor as oxidant. This malic enzyme is critical to the nematode for muscle function under anaerobic conditions. Unlike mammalian versions of the enzyme such as that found in rat liver, which require NADP as cofactor, the nematode version is an NAD-dependent enzyme. We report the crystallization of samples of the nematode enzyme at room temperature from pH 7.5 solutions of polyethylene glycol 4000 containing magnesium sulfate, NAD and sodium tartronate. Immediately upon mixing of protein and precipitant solutions, a marked precipitation of the protein occurs. Out of this precipitate, crystals appear almost immediately, most commonly in a truncated cube form that can grow to 0.5 to 0.7 mm on a cube edge in two to three days. The crystals are trigonal, space group
P3
1
21 or its enantiomer, with
a = b = 131.2(7)
A
̊
, c = 152.6(9)
A
̊
, and two monomers per asymmetric unit. Fresh crystals diffract X-radiation from a synchrotron source (λ = 0.95 Å) to about 3.0 Å resolution. Rotational analysis of Patterson functions indicates that the malic enzyme tetramer has 222 symmetry.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>1640469</pmid><doi>10.1016/0022-2836(92)90971-L</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1992-07, Vol.226 (2), p.565-569 |
| issn | 0022-2836 1089-8638 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Ascaris - enzymology Ascaris suum Biological and medical sciences crystal structure Crystalline structure crystallization Crystallography Fundamental and applied biological sciences. Psychology malate dehydrogenase (oxaloacetate-decarboxylating) Malate Dehydrogenase - chemistry Malate Dehydrogenase - ultrastructure malic enzyme Mitochondria - enzymology Molecular biophysics molecular conformation NAD-dependent parasitic nematode Protein Conformation Structure in molecular biology X-ray diffraction |
| title | Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum |
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