1wpr
From Proteopedia
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| - | [[Image:1wpr.gif|left|200px]] | + | [[Image:1wpr.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of RsbQ inhibited by PMSF''' | + | {{Structure |
| + | |PDB= 1wpr |SIZE=350|CAPTION= <scene name='initialview01'>1wpr</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PMS:BENZYLSULFINIC+ACID'>PMS</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= rsbq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of RsbQ inhibited by PMSF''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WPR is a [ | + | 1WPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15632289 15632289] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta hydrolase]] | [[Category: alpha/beta hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:02 2008'' |
Revision as of 13:00, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | rsbq (Bacillus subtilis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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