1wpr
From Proteopedia
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Crystal structure of RsbQ inhibited by PMSF
Overview
Growth-limiting stresses in bacteria induce the general stress response to, protect the cells against future stresses. Energy stress caused by, starvation conditions in Bacillus subtilis is transmitted to the sigma(B), transcription factor by stress-response regulators. RsbP, a positive, regulator, is a phosphatase containing a PAS (Per-ARNT-Sim) domain and, requires catalytic function of a putative alpha/beta hydrolase, RsbQ, to, be activated. These two proteins have been found to interact with each, other. We determined the crystal structures of RsbQ in native and, inhibitor-bound forms to investigate why RsbP requires RsbQ. These, structures confirm that RsbQ belongs to the alpha/beta hydrolase, superfamily. Since the catalytic triad is buried inside the molecule due, to the closed conformation, the active site is constructed as a, hydrophobic cavity that is nearly isolated from the solvent. This suggests, that RsbQ has specificity for a hydrophobic small compound rather than a, macromolecule such as RsbP. Moreover, structural comparison with other, alpha/beta hydrolases demonstrates that a unique loop region of RsbQ is a, likely candidate for the interaction site with RsbP, and the interaction, might be responsible for product release by operating the hydrophobic gate, equipped between the cavity and the solvent. Our results support the, possibility that RsbQ provides a cofactor molecule for the mature, functionality of RsbP.
About this Structure
1WPR is a Single protein structure of sequence from Bacillus subtilis with PMS and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis., Kaneko T, Tanaka N, Kumasaka T, Protein Sci. 2005 Feb;14(2):558-65. Epub 2005 Jan 4. PMID:15632289
Page seeded by OCA on Wed Nov 21 05:35:26 2007
