4mdt

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{{STRUCTURE_4mdt| PDB=4mdt | SCENE= }}
{{STRUCTURE_4mdt| PDB=4mdt | SCENE= }}
===Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine===
===Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine===
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{{ABSTRACT_PUBMED_24108127}}
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==Function==
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[[http://www.uniprot.org/uniprot/K0BGQ2_ECO1E K0BGQ2_ECO1E]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).[HAMAP-Rule:MF_00388][SAAS:SAAS015870_004_013136]
==About this Structure==
==About this Structure==
[[4mdt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDT OCA].
[[4mdt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDT OCA].
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==Reference==
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<ref group="xtra">PMID:024108127</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Clayton, G M.]]
[[Category: Clayton, G M.]]

Revision as of 05:15, 23 October 2013

Template:STRUCTURE 4mdt

Contents

Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine

Template:ABSTRACT PUBMED 24108127

Function

[K0BGQ2_ECO1E] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).[HAMAP-Rule:MF_00388][SAAS:SAAS015870_004_013136]

About this Structure

4mdt is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Clayton GM, Klein DJ, Rickert KW, Patel SB, Kornienko M, Zugay-Murphy J, Reid JC, Tummala S, Sharma S, Singh SB, Miesel L, Lumb KJ, Soisson SM. Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer. J Biol Chem. 2013 Oct 9. PMID:24108127 doi:http://dx.doi.org/10.1074/jbc.M113.513028

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