1lxa
From Proteopedia
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(New page: 200px<br /><applet load="1lxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxa, resolution 2.6Å" /> '''UDP N-ACETYLGLUCOSAMI...)
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Revision as of 18:50, 20 November 2007
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UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE
Overview
UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer, of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to, UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A, biosynthetic pathway and is a target for the design of antibiotics. The, x-ray crystal structure of LpxA has been determined to 2.6 angstrom, resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold, displays repeated violations of the protein folding constraint requiring, right-handed crossover connections between strands of parallel beta sheets, and may be present in other enzymes that share amino acid sequence, homology to the repeated hexapeptide motif of LpxA.
About this Structure
1LXA is a Single protein structure of sequence from Escherichia coli. Active as [acyl-carrier-protein--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number 2.3.1.129 Full crystallographic information is available from OCA.
Reference
A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase., Raetz CR, Roderick SL, Science. 1995 Nov 10;270(5238):997-1000. PMID:7481807 [[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
Page seeded by OCA on Tue Nov 20 20:57:33 2007
