3IGN

Crystal Structure of the GGDEF domain from Marinobacter aquaeolei diguanylate cyclase complexed with c-di-GMP - Northeast Structural Genomics Consortium Target MqR89a

3IGN の概要

• エントリーDOI: 10.2210/pdb3ign/pdb
• 分子名称: Diguanylate cyclase, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (3 entities in total)
• 機能のキーワード: diguanylate cyclase, ggdef domain, a1u3w3_marav, nesg, mqr89a, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, transferase
• 由来する生物種: Marinobacter aquaeolei VT8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21844.66

構造登録者

Vorobiev, S.,Neely, H.,Seetharaman, J.,Wang, H.,Foote, E.L.,Ciccosanti, C.,Sahdev, S.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (登録日: 2009-07-28, 公開日: 2009-08-11, 最終更新日: 2024-10-30)

主引用文献

Vorobiev, S.M.,Neely, H.,Yu, B.,Seetharaman, J.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Hunt, J.F.
Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product.
J.Struct.Funct.Genom., 13:177-183, 2012

PubMed Abstract: Recent studies of signal transduction in bacteria have revealed a unique second messenger, bis-(3'-5')-cyclic dimeric GMP (c-di-GMP), which regulates transitions between motile states and sessile states, such as biofilms. C-di-GMP is synthesized from two GTP molecules by diguanylate cyclases (DGC). The catalytic activity of DGCs depends on a conserved GG(D/E)EF domain, usually part of a larger multi-domain protein organization. The domains other than the GG(D/E)EF domain often control DGC activation. This paper presents the 1.83 Å crystal structure of an isolated catalytically competent GG(D/E)EF domain from the A1U3W3_MARAV protein from Marinobacter aquaeolei. Co-crystallization with GTP resulted in enzymatic synthesis of c-di-GMP. Comparison with previously solved DGC structures shows a similar orientation of c-di-GMP bound to an allosteric regulatory site mediating feedback inhibition of the enzyme. Biosynthesis of c-di-GMP in the crystallization reaction establishes that the enzymatic activity of this DGC domain does not require interaction with regulatory domains.

PubMed: 22843345
DOI: 10.1007/s10969-012-9136-4

実験手法

X-RAY DIFFRACTION (1.83 Å)