2qiv

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(New page: 200px<br /><applet load="2qiv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qiv, resolution 1.850&Aring;" /> '''Structural basis fo...)
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[[Image:2qiv.jpg|left|200px]]<br /><applet load="2qiv" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qiv, resolution 1.850&Aring;" />
 
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'''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase'''<br />
 
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==Overview==
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==Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase==
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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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<StructureSection load='2qiv' size='340' side='right'caption='[[2qiv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/2qiv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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].
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*[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Escherichia coli K-12]]
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[[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
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[[Category: Large Structures]]
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[[Category: Escherichia coli]]
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[[Category: Raetz CRH]]
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[[Category: Single protein]]
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[[Category: Williams AH]]
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[[Category: Raetz, C.R.H.]]
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[[Category: Williams, A.H.]]
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[[Category: U21]]
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[[Category: left-handed parallel beta helix; protein lipid recognition]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:21:17 2008''
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Current revision

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

PDB ID 2qiv

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