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2qiv

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Revision as of 09:49, 18 October 2017

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

Structural highlights

2qiv is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2qia
Gene:	lpxa (ECOLI)
Activity:	[acyl-carrier-protein--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number 2.3.1.129
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LPXA_ECOLI] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00387]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qiv"

@@ Line 1: / Line 1: @@
 ==Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase==
 <StructureSection load='2qiv' size='340' side='right' caption='[[2qiv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiv OCA], [http://pdbe.org/2qiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qiv RCSB], [http://www.ebi.ac.uk/pdbsum/2qiv PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiv OCA], [http://pdbe.org/2qiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qiv RCSB], [http://www.ebi.ac.uk/pdbsum/2qiv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qiv ProSAT]</span></td></tr>
 </table>
 == Function ==

2qiv

From Proteopedia

Revision as of 09:49, 18 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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