2j65: Difference between revisions

Revision as of 12:20, 28 July 2008

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File:2j65.png

Template:STRUCTURE 2j65

STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDPSTRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP

Template:ABSTRACT PUBMED 17077484

About this StructureAbout this Structure

2J65 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

The nucleotide-binding site of Aquifex aeolicus LpxC., Buetow L, Dawson A, Hunter WN, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1082-6. Epub 2006 Oct 25. PMID:17077484

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP'''
+===STRUCTURE OF LPXC FROM AQUIFEX AEOLICUS IN COMPLEX WITH UDP===
-==Overview==
+<!--
-The structure of recombinant Aquifex aeolicus UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP has been determined to a resolution of 2.2 A. Previous studies have characterized the binding sites of the fatty-acid and sugar moieties of the substrate, UDP-(3-O-hydroxymyristoyl)-N-acetylglucosamine, but not that of the nucleotide. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250. The orientation of the phosphate-ribose tail is not conducive to catalysis, perhaps owing to the position of an inhibitory Zn(2+). However, based on the position of uracil revealed in this study and on the previously reported complex of LpxC with an inhibitor, a model is proposed for substrate binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_17077484}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17077484 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17077484}}
 ==About this Structure==
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 [[Category: Lipid a biosynthesis]]
 [[Category: Lipid synthesis]]
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