Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution

Mickey Kosloff, Gye Won Han, S. Sri Krishna, Robert Schwarzenbacher, Marc Fasnacht, Marc André Elsliger, Polat Abdubek, Sanjay Agarwalla, Eileen Ambing, Tamara Astakhova, Herbert L. Axelrod, Jaume M. Canaves, Dennis Carlton, Hsiu Ju Chiu, Thomas Clayton, Michael DiDonato, Lian Duan, Julie Feuerhelm, Carina Grittini, Slawomir K. GrzechnikJoanna Hale, Eric Hampton, Justin Haugen, Lukasz Jaroszewski, Kevin K. Jin, Hope Johnson, Heath E. Klock, Mark W. Knuth, Eric Koesema, Andreas Kreusch, Peter Kuhn, Inna Levin, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Kin Moy, Edward Nigoghossian, Linda Okach, Silvya Oommachen, Rebecca Page, Jessica Paulsen, Kevin Quijano, Ron Reyes, Christopher L. Rife, Eric Sims, Glen Spraggon, Vandana Sridhar, Raymond C. Stevens, Henry Van Den Bedem, Jeff Velasquez, Aprilfawn White, Guenter Wolf, Qingping Xu, Keith O. Hodgson, John Wooley, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)527-537
Number of pages11
JournalProteins: Structure, Function and Genetics
Volume65
Issue number3
DOIs
StatePublished - 15 Nov 2006
Externally publishedYes

Keywords

  • Active site
  • Consensus sequence
  • Dimer interface
  • Glutathione transferase
  • JCSG
  • Local structural motif
  • Specificity
  • Structural genomics
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology
  • Biochemistry

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