Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii
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. The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotran...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2016, Vol.72 (Pt 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 | 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.
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. |
| doi_str_mv | 10.1107/S2053230X1600978X |
| format | Article |
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T. thermophilus
,
S. tokodaii
and
M. jannaschii
are determined and their structural characteristics are analyzed.
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.</description><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X1600978X</identifier><identifier>PMID: 27487927</identifier><language>eng</language><publisher>International Union of Crystallography</publisher><subject>Research Communications</subject><ispartof>Acta crystallographica. Section F, Structural biology communications, 2016, Vol.72 (Pt 8), p.627-635</ispartof><rights>International Union of Crystallography 2016 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4973304/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4973304/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,4010,27900,27901,27902,53766,53768</link.rule.ids></links><search><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><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><description>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.
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.</description><subject>Research Communications</subject><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNpVj81KAzEUhYMgKuoDuMsDtJpMps3MRpDiH1QUWsHdcCdz04lmkpIfoQ_lxkfwyXTQjavL-b7DgUvIGWfnnDN5sSrYTBSCvfA5Y7WsXvbI0YimIzskpzG-MsbGKpf1ATksZFnJupBH5HMRdjGBpTGFrFIOGKnXFGjMbXYmjSH1SLUPw85-fWzsThkHg-mQBtN6l5VFn8Y4Qp8CuKgxQMQJfcphNaE6-IGuewxDjuNWGPy2NzbHCV1lq7317Sj8m-_AGAquow-YenBege288kr9-FdwDqLqjTkh-xpsxNO_e0yeb67Xi7vp8vH2fnG1nG55PUtTAFZI1EwwxaFSUtTYCs1rFMVshho6gQKrOWqEWihoUbKyrLpWzctC64KLY3L5u7vN7YCdQvfznG22wQwQdo0H0_w3zvTNxr83ZS2FYKX4BlimhjE</recordid><startdate>2016</startdate><enddate>2016</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>5PM</scope></search><sort><creationdate>2016</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-p195t-aa027ef030c1a8c739eb3f19e3255efad3e3e86efea93cabe70448dbc642ff213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Research Communications</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><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>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><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><date>2016</date><risdate>2016</risdate><volume>72</volume><issue>Pt 8</issue><spage>627</spage><epage>635</epage><pages>627-635</pages><eissn>2053-230X</eissn><abstract>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.
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.</abstract><pub>International Union of Crystallography</pub><pmid>27487927</pmid><doi>10.1107/S2053230X1600978X</doi><tpages>9</tpages></addata></record> |
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| subjects | Research Communications |
| title | Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii |
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