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| - | [[Image:1txk.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1txk.png|left|200px]] |
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| | {{STRUCTURE_1txk| PDB=1txk | SCENE= }} | | {{STRUCTURE_1txk| PDB=1txk | SCENE= }} |
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| - | '''Crystal structure of Escherichia coli OpgG'''
| + | ===Crystal structure of Escherichia coli OpgG=== |
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| - | ==Overview==
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| - | Osmoregulated periplasmic glucans (OPGs) G protein (OpgG) is required for OPGs biosynthesis. OPGs from Escherichia coli are branched glucans, with a backbone of beta-1,2 glucose units and with branches attached by beta-1,6 linkages. In Proteobacteria, OPGs are involved in osmoprotection, biofilm formation, virulence and resistance to antibiotics. Despite their important biological implications, enzymes synthesizing OPGs are poorly characterized. Here, we report the 2.5 A crystal structure of OpgG from E.coli. The structure was solved using a selenemethionine derivative of OpgG and the multiple anomalous diffraction method (MAD). The protein is composed of two beta-sandwich domains connected by one turn of 3(10) helix. The N-terminal domain (residues 22-388) displays a 25-stranded beta-sandwich fold found in several carbohydrate-related proteins. It exhibits a large cleft comprising many aromatic and acidic residues. This putative binding site shares some similarities with enzymes such as galactose mutarotase and glucodextranase, suggesting a potential catalytic role for this domain in OPG synthesis. On the other hand, the C-terminal domain (residues 401-512) has a seven-stranded immunoglobulin-like beta-sandwich fold, found in many proteins where it is mainly implicated in interactions with other molecules. The structural data suggest that OpgG is an OPG branching enzyme in which the catalytic activity is located in the large N-terminal domain and controlled via the smaller C-terminal domain.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15313617}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15313617 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15313617}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Villeret, V.]] | | [[Category: Villeret, V.]] |
| | [[Category: Beta-sandwich]] | | [[Category: Beta-sandwich]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:29:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:40:50 2008'' |
Revision as of 04:41, 28 July 2008
Template:STRUCTURE 1txk
Crystal structure of Escherichia coli OpgG
Template:ABSTRACT PUBMED 15313617
About this Structure
1TXK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans., Hanoulle X, Rollet E, Clantin B, Landrieu I, Odberg-Ferragut C, Lippens G, Bohin JP, Villeret V, J Mol Biol. 2004 Sep 3;342(1):195-205. PMID:15313617
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