2oi6: Difference between revisions

Revision as of 08:38, 28 July 2008

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File:2oi6.png

Template:STRUCTURE 2oi6

E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4

Template:ABSTRACT PUBMED 17473010

About this StructureAbout this Structure

2OI6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products., Olsen LR, Vetting MW, Roderick SL, Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. PMID:17473010

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-'''E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4'''
+===E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4===
-==Overview==
+<!--
-The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_17473010}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17473010 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17473010}}
 ==About this Structure==
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 [[Category: Vetting, M W.]]
 [[Category: Left-handed beta helix]]
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