2qiv: Difference between revisions

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[[Image:2qiv.jpg|left|200px]]<br /><applet load="2qiv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2qiv, resolution 1.850&Aring;" />
'''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase'''<br />


==Overview==
==Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase==
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.
<StructureSection load='2qiv' size='340' side='right'caption='[[2qiv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2qiv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QIV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U21:URIDINE-5-DIPHOSPHATE-3-O-(R-3-HYDROXYDECANOYL)-N-ACETYL-D-GLUCOSAMINE'>U21</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiv OCA], [https://pdbe.org/2qiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qiv RCSB], [https://www.ebi.ac.uk/pdbsum/2qiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qiv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LPXA_ECOLI 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/2qiv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qiv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2QIV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=U21:'>U21</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIV OCA].
*[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698807 17698807]
[[Category: Escherichia coli K-12]]
[[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
[[Category: Large Structures]]
[[Category: Escherichia coli]]
[[Category: Raetz CRH]]
[[Category: Single protein]]
[[Category: Williams AH]]
[[Category: Raetz, C R.H.]]
[[Category: Williams, A H.]]
[[Category: U21]]
[[Category: left-handed parallel beta helix; protein lipid recognition]]
[[Category: transferase]]
 
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Retrieved from "https://proteopedia.org/2qiv"