Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii
The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2016-08, Vol.72 (8), p.627-635 |
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| creator | Watanabe, Yuzo Yanai, Hisaaki Kanagawa, Mayumi Suzuki, Sakiko Tamura, Satoko Okada, Kiyoshi Baba, Seiki Kumasaka, Takashi Agari, Yoshihiro Chen, Lirong Fu, Zheng-Qing Chrzas, John Wang, Bi-Cheng Nakagawa, Noriko Ebihara, Akio Masui, Ryoji Kuramitsu, Seiki Yokoyama, Shigeyuki Sampei, Gen-ichi Kawai, Gota |
| description | The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular‐dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion.
Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from T. thermophilus, S. tokodaii and M. jannaschii are determined and their structural characteristics are analyzed. |
| doi_str_mv | 10.1107/S2053230X1600978X |
| format | Article |
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Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from T. thermophilus, S. tokodaii and M. jannaschii are determined and their structural characteristics are analyzed.</description><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X1600978X</identifier><identifier>PMID: 27487927</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - chemistry ; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - genetics ; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - metabolism ; Cloning, Molecular ; crystal structure ; Crystallography, X-Ray ; Escherichia coli - genetics ; Escherichia coli - metabolism ; formylglycinamide ribonucleotide amidotransferase ; Gene Expression ; Methanocaldococcus - chemistry ; Methanocaldococcus - enzymology ; Methanocaldococcus jannaschii ; Models, Molecular ; Molecular Dynamics Simulation ; Plasmids - chemistry ; Plasmids - metabolism ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; purine nucleotide-biosynthetic pathway ; PurS ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sulfolobus - chemistry ; Sulfolobus - enzymology ; Sulfolobus tokodaii ; Thermus thermophilus ; Thermus thermophilus - chemistry ; Thermus thermophilus - enzymology</subject><ispartof>Acta crystallographica. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii</title><title>Acta crystallographica. Section F, Structural biology communications</title><addtitle>Acta Cryst. F</addtitle><description>The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular‐dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion.
Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from T. thermophilus, S. tokodaii and M. jannaschii are determined and their structural characteristics are analyzed.</description><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - chemistry</subject><subject>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - genetics</subject><subject>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - metabolism</subject><subject>Cloning, Molecular</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>formylglycinamide ribonucleotide amidotransferase</subject><subject>Gene Expression</subject><subject>Methanocaldococcus - chemistry</subject><subject>Methanocaldococcus - enzymology</subject><subject>Methanocaldococcus jannaschii</subject><subject>Models, Molecular</subject><subject>Molecular Dynamics Simulation</subject><subject>Plasmids - chemistry</subject><subject>Plasmids - metabolism</subject><subject>Protein Binding</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Conformation, beta-Strand</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>purine nucleotide-biosynthetic pathway</subject><subject>PurS</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sulfolobus - chemistry</subject><subject>Sulfolobus - enzymology</subject><subject>Sulfolobus tokodaii</subject><subject>Thermus thermophilus</subject><subject>Thermus thermophilus - chemistry</subject><subject>Thermus thermophilus - enzymology</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSMEolXpA7BBFisWE7DjJJ4s2xEtSAMUzSAKG8txrolbxx78I8hb8YgkSqmQWLCy77nnO4t7suwpwS8JwezVrsAVLSi-JjXGDVtfP8iOZymftYd__Y-y0xBuMMYzRljzODsqWLlmTcGOs18bP4YoDArRJxmTh4CcQgKF1Car4zzEHpByfhjNNzNKbcWgO0Bet84macDFeZxFF72wQYEXAVboKvndCinvBrTvwQ8pzEl-cIdemxRWaJeMcsa188Lduk5ojYTt0DuIvbBOCtM56aSc9jfCWhFkr_WT7JESJsDp3XuSfbp4vd-8ybcfLt9uzra5pGVNcgHAiCwZJYJhDE1H6wJLogitSYsbpVqogTIq60IWtSqL6YSims6D1wy3uKQn2fMl14WoeZA6guylsxZk5IQWJaubyfRiMR28-54gRD7oIMEYYcGlwMkaN1M7tF5PVrJYpXcheFD84PUg_MgJ5nMz_J9CJ-bZXXxqB-juiT_1TYZmMfzQBsb_J_KzLxfF_rwimExsvrA6RPh5zwp_y2tGWcU_v7_kFH-szrflV35FfwP5xb7T</recordid><startdate>201608</startdate><enddate>201608</enddate><creator>Watanabe, Yuzo</creator><creator>Yanai, Hisaaki</creator><creator>Kanagawa, Mayumi</creator><creator>Suzuki, Sakiko</creator><creator>Tamura, Satoko</creator><creator>Okada, Kiyoshi</creator><creator>Baba, Seiki</creator><creator>Kumasaka, Takashi</creator><creator>Agari, Yoshihiro</creator><creator>Chen, Lirong</creator><creator>Fu, Zheng-Qing</creator><creator>Chrzas, John</creator><creator>Wang, Bi-Cheng</creator><creator>Nakagawa, Noriko</creator><creator>Ebihara, Akio</creator><creator>Masui, Ryoji</creator><creator>Kuramitsu, Seiki</creator><creator>Yokoyama, Shigeyuki</creator><creator>Sampei, Gen-ichi</creator><creator>Kawai, Gota</creator><general>International Union of Crystallography</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>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>201608</creationdate><title>Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii</title><author>Watanabe, Yuzo ; Yanai, Hisaaki ; Kanagawa, Mayumi ; Suzuki, Sakiko ; Tamura, Satoko ; Okada, Kiyoshi ; Baba, Seiki ; Kumasaka, Takashi ; Agari, Yoshihiro ; Chen, Lirong ; Fu, Zheng-Qing ; Chrzas, John ; Wang, Bi-Cheng ; Nakagawa, Noriko ; Ebihara, Akio ; Masui, Ryoji ; Kuramitsu, Seiki ; Yokoyama, Shigeyuki ; Sampei, Gen-ichi ; Kawai, Gota</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3461-aee71c4731a700e9d3620c1f1361b09ffbe6e373c62c26f42097a57170870b043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - chemistry</topic><topic>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - genetics</topic><topic>Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - metabolism</topic><topic>Cloning, Molecular</topic><topic>crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>formylglycinamide ribonucleotide amidotransferase</topic><topic>Gene Expression</topic><topic>Methanocaldococcus - chemistry</topic><topic>Methanocaldococcus - enzymology</topic><topic>Methanocaldococcus jannaschii</topic><topic>Models, Molecular</topic><topic>Molecular Dynamics Simulation</topic><topic>Plasmids - chemistry</topic><topic>Plasmids - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Conformation, beta-Strand</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>purine nucleotide-biosynthetic pathway</topic><topic>PurS</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sulfolobus - chemistry</topic><topic>Sulfolobus - enzymology</topic><topic>Sulfolobus tokodaii</topic><topic>Thermus thermophilus</topic><topic>Thermus thermophilus - chemistry</topic><topic>Thermus thermophilus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Yuzo</creatorcontrib><creatorcontrib>Yanai, Hisaaki</creatorcontrib><creatorcontrib>Kanagawa, Mayumi</creatorcontrib><creatorcontrib>Suzuki, Sakiko</creatorcontrib><creatorcontrib>Tamura, Satoko</creatorcontrib><creatorcontrib>Okada, Kiyoshi</creatorcontrib><creatorcontrib>Baba, Seiki</creatorcontrib><creatorcontrib>Kumasaka, Takashi</creatorcontrib><creatorcontrib>Agari, Yoshihiro</creatorcontrib><creatorcontrib>Chen, Lirong</creatorcontrib><creatorcontrib>Fu, Zheng-Qing</creatorcontrib><creatorcontrib>Chrzas, John</creatorcontrib><creatorcontrib>Wang, Bi-Cheng</creatorcontrib><creatorcontrib>Nakagawa, Noriko</creatorcontrib><creatorcontrib>Ebihara, Akio</creatorcontrib><creatorcontrib>Masui, Ryoji</creatorcontrib><creatorcontrib>Kuramitsu, Seiki</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><creatorcontrib>Sampei, Gen-ichi</creatorcontrib><creatorcontrib>Kawai, Gota</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</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>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Yuzo</au><au>Yanai, Hisaaki</au><au>Kanagawa, Mayumi</au><au>Suzuki, Sakiko</au><au>Tamura, Satoko</au><au>Okada, Kiyoshi</au><au>Baba, Seiki</au><au>Kumasaka, Takashi</au><au>Agari, Yoshihiro</au><au>Chen, Lirong</au><au>Fu, Zheng-Qing</au><au>Chrzas, John</au><au>Wang, Bi-Cheng</au><au>Nakagawa, Noriko</au><au>Ebihara, Akio</au><au>Masui, Ryoji</au><au>Kuramitsu, Seiki</au><au>Yokoyama, Shigeyuki</au><au>Sampei, Gen-ichi</au><au>Kawai, Gota</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii</atitle><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2016-08</date><risdate>2016</risdate><volume>72</volume><issue>8</issue><spage>627</spage><epage>635</epage><pages>627-635</pages><issn>2053-230X</issn><eissn>2053-230X</eissn><abstract>The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular‐dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion.
Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from T. thermophilus, S. tokodaii and M. jannaschii are determined and their structural characteristics are analyzed.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>27487927</pmid><doi>10.1107/S2053230X1600978X</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 2053-230X |
| ispartof | Acta crystallographica. Section F, Structural biology communications, 2016-08, Vol.72 (8), p.627-635 |
| issn | 2053-230X 2053-230X |
| language | eng |
| recordid | cdi_osti_scitechconnect_1324769 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - chemistry Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - genetics Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor - metabolism Cloning, Molecular crystal structure Crystallography, X-Ray Escherichia coli - genetics Escherichia coli - metabolism formylglycinamide ribonucleotide amidotransferase Gene Expression Methanocaldococcus - chemistry Methanocaldococcus - enzymology Methanocaldococcus jannaschii Models, Molecular Molecular Dynamics Simulation Plasmids - chemistry Plasmids - metabolism Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Multimerization Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism purine nucleotide-biosynthetic pathway PurS Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Sulfolobus - chemistry Sulfolobus - enzymology Sulfolobus tokodaii Thermus thermophilus Thermus thermophilus - chemistry Thermus thermophilus - enzymology |
| title | Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T11%3A45%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structures%20of%20a%20subunit%20of%20the%20formylglycinamide%20ribonucleotide%20amidotransferase,%20PurS,%20from%20Thermus%20thermophilus,%20Sulfolobus%20tokodaii%20and%20Methanocaldococcus%20jannaschii&rft.jtitle=Acta%20crystallographica.%20Section%20F,%20Structural%20biology%20communications&rft.au=Watanabe,%20Yuzo&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2016-08&rft.volume=72&rft.issue=8&rft.spage=627&rft.epage=635&rft.pages=627-635&rft.issn=2053-230X&rft.eissn=2053-230X&rft_id=info:doi/10.1107/S2053230X1600978X&rft_dat=%3Cproquest_osti_%3E1809600368%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1809600368&rft_id=info:pmid/27487927&rfr_iscdi=true |