4e79

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e79]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E79 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e79]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E79 FirstGlance]. <br>
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</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=4e79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e79 OCA], [https://pdbe.org/4e79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e79 RCSB], [https://www.ebi.ac.uk/pdbsum/4e79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e79 ProSAT]</span></td></tr>
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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]] 2.66&#8491;</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=4e79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e79 OCA], [https://pdbe.org/4e79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e79 RCSB], [https://www.ebi.ac.uk/pdbsum/4e79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e79 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LPXD_ACIBS LPXD_ACIBS]] Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00523]
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[https://www.uniprot.org/uniprot/LPXD_ACIBS LPXD_ACIBS] Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[HAMAP-Rule:MF_00523]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acinetobacter baumannii is a Gram-negative bacterium that is resistant to many currently available antibiotics. The protein LpxD is a component of the biosynthetic pathway for lipopolysaccharides in the outer membrane of this bacterium and is a potential target for new antibacterial agents. This paper describes the structure determination of apo forms of LpxD in space groups P2(1) and P4(3)22. These crystals contained six and three copies of the protein molecule in the asymmetric unit and diffracted to 2.8 and 2.7 A resolution, respectively. A comparison of the multiple protein copies in the asymmetric units of these crystals reveals a common protein conformation and a conformation in which the relative orientation between the two major domains in the protein is altered.
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Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.,Badger J, Chie-Leon B, Logan C, Sridhar V, Sankaran B, Zwart PH, Nienaber V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):6-9. doi:, 10.1107/S1744309112048890. Epub 2012 Dec 25. PMID:23295477<ref>PMID:23295477</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4e79" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase]]
*[[UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase]]
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== References ==
 
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<references/>
 
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</StructureSection>
</StructureSection>

Current revision

Structure of LpxD from Acinetobacter baumannii at 2.66A resolution (P4322 form)

PDB ID 4e79

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