2FNO

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

「1ZGM」から置き換えられました

2FNO の概要

• エントリーDOI: 10.2210/pdb2fno/pdb
• 分子名称: AGR_pAT_752p, THIOCYANATE ION (3 entities in total)
• 機能のキーワード: thioredoxin fold, gst c-terminal domain-like fold, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, transferase
• 由来する生物種: Agrobacterium tumefaciens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56029.54

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2006-01-11, 公開日: 2006-02-14, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)