2o7l: Difference between revisions

Revision as of 02:27, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2o7l.png

Template:STRUCTURE 2o7l

The open-cap conformation of GlpGThe open-cap conformation of GlpG

Template:ABSTRACT PUBMED 17277078

About this StructureAbout this Structure

2O7L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Open-cap conformation of intramembrane protease GlpG., Wang Y, Ha Y, Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2098-102. Epub 2007 Feb 2. PMID:17277078

Page seeded by OCA on Mon Jul 28 02:26:58 2008

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OCA

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-'''The open-cap conformation of GlpG'''
+===The open-cap conformation of GlpG===
-==Overview==
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-The active sites of intramembrane proteases are positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane. Previous crystallographic analysis of Escherichia coli GlpG, an intramembrane protease of the rhomboid family, has revealed an internal and hydrophilic active site in an apparently closed conformation. Here we describe the crystal structure of GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser-201 to outside aqueous solution. A water molecule now moves into the putative oxyanion hole that is constituted of a main-chain amide (Ser-201) and two conserved side chains (His-150 and Asn-154). The loop movement also destabilizes a hydrophobic side chain (Phe-245) previously buried between transmembrane helices S2 and S5 and creates a side portal from the lipid to protease active site. These results provide insights into the conformational plasticity of GlpG to accommodate substrate binding and catalysis and into the chirality of the reaction intermediate.
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 [[Category: Membrane protein]]
 [[Category: Rhomboid protease]]
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