2QTP

Crystal structure of a duf1185 family protein (spo0826) from silicibacter pomeroyi dss-3 at 2.10 A resolution

2QTP の概要

• エントリーDOI: 10.2210/pdb2qtp/pdb
• 分子名称: Uncharacterized protein (2 entities in total)
• 機能のキーワード: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, unknown function
• 由来する生物種: Silicibacter pomeroyi DSS-3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20812.06

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2007-08-02, 公開日: 2007-08-21, 最終更新日: 2024-10-30)

主引用文献

Bakolitsa, C.,Kumar, A.,Jin, K.K.,McMullan, D.,Krishna, S.S.,Miller, M.D.,Abdubek, P.,Acosta, C.,Astakhova, T.,Axelrod, H.L.,Burra, P.,Carlton, D.,Chen, C.,Chiu, H.J.,Clayton, T.,Das, D.,Deller, M.C.,Duan, L.,Elias, Y.,Ellrott, K.,Ernst, D.,Farr, C.L.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Grzechnik, S.K.,Han, G.W.,Jaroszewski, L.,Johnson, H.A.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Marciano, D.,Morse, A.T.,Murphy, K.D.,Nigoghossian, E.,Nopakun, A.,Okach, L.,Paulsen, J.,Puckett, C.,Reyes, R.,Rife, C.L.,Sefcovic, N.,Tien, H.J.,Trame, C.B.,Trout, C.V.,van den Bedem, H.,Weekes, D.,White, A.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism.
Acta Crystallogr.,Sect.F, 66:1182-1189, 2010

PubMed Abstract: The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.

PubMed: 20944209
DOI: 10.1107/S1744309109050647

実験手法

X-RAY DIFFRACTION (2.1 Å)