2o7l
From Proteopedia
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| - | [[Image:2o7l.gif|left|200px]] | + | [[Image:2o7l.gif|left|200px]] |
| - | + | ||
| - | '''The open-cap conformation of GlpG''' | + | {{Structure |
| + | |PDB= 2o7l |SIZE=350|CAPTION= <scene name='initialview01'>2o7l</scene>, resolution 2.500Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''The open-cap conformation of GlpG''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O7L is a [ | + | 2O7L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7L OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17277078 17277078] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rhomboid protease]] | [[Category: rhomboid protease]] | ||
| - | ''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 17:56:06 2008'' |
Revision as of 15:56, 20 March 2008
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| , resolution 2.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | glpG (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The open-cap conformation of GlpG
Overview
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.
About this Structure
2O7L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 17:56:06 2008
