2FNO

Crystal structure of a glutathione s-transferase (atu5508) from agrobacterium tumefaciens str. c58 at 2.00 A resolution

Replaces:  1ZGM

Summary for 2FNO

• Entry DOI: 10.2210/pdb2fno/pdb
• Descriptor: AGR_pAT_752p, THIOCYANATE ION (3 entities in total)
• Functional Keywords: thioredoxin fold, gst c-terminal domain-like fold, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, transferase
• Biological source: Agrobacterium tumefaciens
• Total number of polymer chains: 2
• Total formula weight: 56029.54

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2006-01-11, release date: 2006-02-14, Last modification date: 2024-11-20)

Primary citation

Kosloff, M.,Han, G.W.,Krishna, S.S.,Schwarzenbacher, R.,Fasnacht, M.,Elsliger, M.A.,Abdubek, P.,Agarwalla, S.,Ambing, E.,Astakhova, T.,Axelrod, H.L.,Canaves, J.M.,Carlton, D.,Chiu, H.J.,Clayton, T.,DiDonato, M.,Duan, L.,Feuerhelm, J.,Grittini, C.,Grzechnik, S.K.,Hale, J.,Hampton, E.,Haugen, J.,Jaroszewski, L.,Jin, K.K.,Johnson, H.,Klock, H.E.,Knuth, M.W.,Koesema, E.,Kreusch, A.,Kuhn, P.,Levin, I.,McMullan, D.,Miller, M.D.,Morse, A.T.,Moy, K.,Nigoghossian, E.,Okach, L.,Oommachen, S.,Page, R.,Paulsen, J.,Quijano, K.,Reyes, R.,Rife, C.L.,Sims, E.,Spraggon, G.,Sridhar, V.,Stevens, R.C.,van den Bedem, H.,Velasquez, J.,White, A.,Wolf, G.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution.
Proteins, 65:527-537, 2006

PubMed 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.

PubMed: 16988933
DOI: 10.1002/prot.21130

Experimental method

X-RAY DIFFRACTION (2 Å)