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New page: left|200px<br /><applet load="1lxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxa, resolution 2.6Å" /> '''UDP N-ACETYLGLUCOSAMI...
 
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[[Image:1lxa.jpg|left|200px]]<br /><applet load="1lxa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lxa, resolution 2.6&Aring;" />
'''UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE'''<br />


==Overview==
==UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE==
UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer, of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to, UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A, biosynthetic pathway and is a target for the design of antibiotics. The, x-ray crystal structure of LpxA has been determined to 2.6 angstrom, resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold, displays repeated violations of the protein folding constraint requiring, right-handed crossover connections between strands of parallel beta sheets, and may be present in other enzymes that share amino acid sequence, homology to the repeated hexapeptide motif of LpxA.
<StructureSection load='1lxa' size='340' side='right'caption='[[1lxa]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lxa]] 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=1LXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LXA 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]] 2.6&#8491;</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=1lxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxa OCA], [https://pdbe.org/1lxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lxa RCSB], [https://www.ebi.ac.uk/pdbsum/1lxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxa 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/lx/1lxa_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=1lxa ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LXA OCA].
*[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]]
 
__TOC__
==Reference==
</StructureSection>
A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase., Raetz CR, Roderick SL, Science. 1995 Nov 10;270(5238):997-1000. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7481807 7481807]
[[Category: Escherichia coli K-12]]
[[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
[[Category: Large Structures]]
[[Category: Escherichia coli]]
[[Category: Roderick SL]]
[[Category: Single protein]]
[[Category: Roderick, S.L.]]
[[Category: acyltransferase]]
[[Category: lipid a biosynthesis]]
[[Category: lipid synthesis]]
[[Category: transferase]]
 
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Retrieved from "https://proteopedia.org/1lxa"