2P4B

Crystal structure of E.coli RseB

2P4B の概要

• エントリーDOI: 10.2210/pdb2p4b/pdb
• 分子名称: Sigma-E factor regulatory protein rseB, octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: open and closed form, signaling protein
• 由来する生物種: Escherichia coli K12
• 細胞内の位置: Periplasm (Potential): P0AFX9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 100278.62

構造登録者

Kim, D.Y.,Kim, K.K. (登録日: 2007-03-12, 公開日: 2007-05-22, 最終更新日: 2024-03-13)

主引用文献

Kim, D.Y.,Jin, K.S.,Kwon, E.,Ree, M.,Kim, K.K.
Crystal structure of RseB and a model of its binding mode to RseA
Proc.Natl.Acad.Sci.Usa, 104:8779-8784, 2007

PubMed Abstract: The bacterial envelope stress response senses stress signals in the extracytoplasmic compartment, and activates sigma(E)-dependent transcription by degrading its antisigma factor RseA. RseB, a binding partner of RseA, plays a pivotal role in regulating this response, but its molecular mechanism is not understood. We therefore determined the crystal structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is composed of two domains linked by a flexible linker and forms a loosely packed dimer with two grooves on each side. This structural feature is confirmed by small-angle scattering in solution. Analysis of the binding of various RseA mutants to RseB allowed us to identify the major RseB-binding motif in RseA. These data, coupled with analysis of small-angle scattering of the RseA/RseB complex in solution, leads us to propose that two RseAs bind to the grooves of the dimeric RseB by conserved residues. The implications for modulating proteolytic cleavage of RseA are discussed.

PubMed: 17496148
DOI: 10.1073/pnas.0703117104

実験手法

X-RAY DIFFRACTION (2.4 Å)