Comparative structural analysis of a novel glutathione S ‐transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 Å resolution
Glutathione S ‐transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small‐molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology to...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2006-11, Vol.65 (3), p.527-537 |
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| creator | Kosloff, Mickey Han, Gye Won Krishna, S. Sri Schwarzenbacher, Robert Fasnacht, Marc Elsliger, Marc‐André Abdubek, Polat Agarwalla, Sanjay Ambing, Eileen Astakhova, Tamara Axelrod, Herbert L. Canaves, Jaume M. Carlton, Dennis Chiu, Hsiu‐Ju Clayton, Thomas DiDonato, Michael Duan, Lian Feuerhelm, Julie Grittini, Carina Grzechnik, Slawomir K. Hale, Joanna Hampton, Eric Haugen, Justin Jaroszewski, Lukasz Jin, Kevin K. Johnson, Hope Klock, Heath E. Knuth, Mark W. Koesema, Eric Kreusch, Andreas Kuhn, Peter Levin, Inna McMullan, Daniel Miller, Mitchell D. Morse, Andrew T. Moy, Kin Nigoghossian, Edward Okach, Linda Oommachen, Silvya Page, Rebecca Paulsen, Jessica Quijano, Kevin Reyes, Ron Rife, Christopher L. Sims, Eric Spraggon, Glen Sridhar, Vandana Stevens, Raymond C. van den Bedem, Henry Velasquez, Jeff White, Aprilfawn Wolf, Guenter Xu, Qingping Hodgson, Keith O. Wooley, John Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. |
| description | Glutathione
S
‐transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small‐molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high‐resolution X‐ray structure of Atu5508 from the pathogenic soil bacterium
Agrobacterium tumefaciens
(atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies. Proteins 2006. © 2006 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/prot.21130 |
| format | Article |
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‐transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small‐molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high‐resolution X‐ray structure of Atu5508 from the pathogenic soil bacterium
Agrobacterium tumefaciens
(atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies. Proteins 2006. © 2006 Wiley‐Liss, Inc.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/prot.21130</identifier><language>eng</language><ispartof>Proteins, structure, function, and bioinformatics, 2006-11, Vol.65 (3), p.527-537</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c146t-c26bf83f8304661e1dab478588b14049166009e2939dc2930e6b0b1f11f7eed63</citedby><cites>FETCH-LOGICAL-c146t-c26bf83f8304661e1dab478588b14049166009e2939dc2930e6b0b1f11f7eed63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Kosloff, Mickey</creatorcontrib><creatorcontrib>Han, Gye Won</creatorcontrib><creatorcontrib>Krishna, S. Sri</creatorcontrib><creatorcontrib>Schwarzenbacher, Robert</creatorcontrib><creatorcontrib>Fasnacht, Marc</creatorcontrib><creatorcontrib>Elsliger, Marc‐André</creatorcontrib><creatorcontrib>Abdubek, Polat</creatorcontrib><creatorcontrib>Agarwalla, Sanjay</creatorcontrib><creatorcontrib>Ambing, Eileen</creatorcontrib><creatorcontrib>Astakhova, Tamara</creatorcontrib><creatorcontrib>Axelrod, Herbert L.</creatorcontrib><creatorcontrib>Canaves, Jaume M.</creatorcontrib><creatorcontrib>Carlton, Dennis</creatorcontrib><creatorcontrib>Chiu, Hsiu‐Ju</creatorcontrib><creatorcontrib>Clayton, Thomas</creatorcontrib><creatorcontrib>DiDonato, Michael</creatorcontrib><creatorcontrib>Duan, Lian</creatorcontrib><creatorcontrib>Feuerhelm, Julie</creatorcontrib><creatorcontrib>Grittini, Carina</creatorcontrib><creatorcontrib>Grzechnik, Slawomir K.</creatorcontrib><creatorcontrib>Hale, Joanna</creatorcontrib><creatorcontrib>Hampton, Eric</creatorcontrib><creatorcontrib>Haugen, Justin</creatorcontrib><creatorcontrib>Jaroszewski, Lukasz</creatorcontrib><creatorcontrib>Jin, Kevin K.</creatorcontrib><creatorcontrib>Johnson, Hope</creatorcontrib><creatorcontrib>Klock, Heath E.</creatorcontrib><creatorcontrib>Knuth, Mark W.</creatorcontrib><creatorcontrib>Koesema, Eric</creatorcontrib><creatorcontrib>Kreusch, Andreas</creatorcontrib><creatorcontrib>Kuhn, Peter</creatorcontrib><creatorcontrib>Levin, Inna</creatorcontrib><creatorcontrib>McMullan, Daniel</creatorcontrib><creatorcontrib>Miller, Mitchell D.</creatorcontrib><creatorcontrib>Morse, Andrew T.</creatorcontrib><creatorcontrib>Moy, Kin</creatorcontrib><creatorcontrib>Nigoghossian, Edward</creatorcontrib><creatorcontrib>Okach, Linda</creatorcontrib><creatorcontrib>Oommachen, Silvya</creatorcontrib><creatorcontrib>Page, Rebecca</creatorcontrib><creatorcontrib>Paulsen, Jessica</creatorcontrib><creatorcontrib>Quijano, Kevin</creatorcontrib><creatorcontrib>Reyes, Ron</creatorcontrib><creatorcontrib>Rife, Christopher L.</creatorcontrib><creatorcontrib>Sims, Eric</creatorcontrib><creatorcontrib>Spraggon, Glen</creatorcontrib><creatorcontrib>Sridhar, Vandana</creatorcontrib><creatorcontrib>Stevens, Raymond C.</creatorcontrib><creatorcontrib>van den Bedem, Henry</creatorcontrib><creatorcontrib>Velasquez, Jeff</creatorcontrib><creatorcontrib>White, Aprilfawn</creatorcontrib><creatorcontrib>Wolf, Guenter</creatorcontrib><creatorcontrib>Xu, Qingping</creatorcontrib><creatorcontrib>Hodgson, Keith O.</creatorcontrib><creatorcontrib>Wooley, John</creatorcontrib><creatorcontrib>Deacon, Ashley M.</creatorcontrib><creatorcontrib>Godzik, Adam</creatorcontrib><creatorcontrib>Lesley, Scott A.</creatorcontrib><creatorcontrib>Wilson, Ian A.</creatorcontrib><title>Comparative structural analysis of a novel glutathione S ‐transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 Å resolution</title><title>Proteins, structure, function, and bioinformatics</title><description>Glutathione
S
‐transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small‐molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high‐resolution X‐ray structure of Atu5508 from the pathogenic soil bacterium
Agrobacterium tumefaciens
(atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies. 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S
‐transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small‐molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high‐resolution X‐ray structure of Atu5508 from the pathogenic soil bacterium
Agrobacterium tumefaciens
(atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies. Proteins 2006. © 2006 Wiley‐Liss, Inc.</abstract><doi>10.1002/prot.21130</doi><tpages>11</tpages></addata></record> |
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| ispartof | Proteins, structure, function, and bioinformatics, 2006-11, Vol.65 (3), p.527-537 |
| issn | 0887-3585 1097-0134 |
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| source | Wiley Online Library Journals Frontfile Complete |
| title | Comparative structural analysis of a novel glutathione S ‐transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 Å resolution |
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