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2qiv

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{{STRUCTURE_2qiv| PDB=2qiv | SCENE= }}
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'''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase'''
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===Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase===
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==Overview==
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UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the reversible transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein to the glucosamine 3-OH group of UDP-GlcNAc. Escherichia coli LpxA is highly selective for R-3-hydroxymyristate. The crystal structure of the E. coli LpxA homotrimer, determined previously in the absence of lipid substrates or products, revealed that LpxA contains an unusual, left-handed parallel beta-helix fold. We have now solved the crystal structures of E. coli LpxA with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc at a resolution of 1.74 A and with bound UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc at 1.85 A. The structures of these complexes are consistent with the catalytic mechanism deduced by mutagenesis and with a recent 3.0-A structure of LpxA with bound UDP-GlcNAc. Our structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding.
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{{ABSTRACT_PUBMED_17698807}}
==About this Structure==
==About this Structure==
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[[Category: Protein lipid recognition]]
[[Category: Protein lipid recognition]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:02:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:51:48 2008''

Revision as of 10:51, 27 July 2008

Image:2qiv.png

Template:STRUCTURE 2qiv

Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase

Template:ABSTRACT PUBMED 17698807

About this Structure

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

Reference

Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase., Williams AH, Raetz CR, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13543-50. Epub 2007 Aug 13. PMID:17698807

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