1MU4

CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)

1MU4 の概要

• エントリーDOI: 10.2210/pdb1mu4/pdb
• 関連するPDBエントリー: 1MO1
• 分子名称: HPr-like protein crh, SULFATE ION (3 entities in total)
• 機能のキーワード: open-faced b-sandwich, phosphotransferase system, swapping domain, transport protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19444.09

構造登録者

Juy, M.R.,Haser, R. (登録日: 2002-09-23, 公開日: 2003-10-07, 最終更新日: 2024-02-14)

主引用文献

Juy, M.R.,Penin, F.,Favier, A.,Galinier, A.,Montserret, R.,Haser, R.,Deutscher, J.,Bockmann, A.
Dimerization of Crh by reversible 3D Domain Swapping Induces Structural Adjustments to its monomeric homologue HPR
J.Mol.Biol., 332:767-776, 2003

PubMed Abstract: The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity.

PubMed: 12972249
DOI: 10.1016/S0022-2836(03)00918-5

実験手法

X-RAY DIFFRACTION (1.8 Å)