View source for 3p76


==X-ray crystal structure of Aquifex aeolicus LpxC complexed SCH1379777==
<StructureSection load='3p76' size='340' side='right'caption='[[3p76]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3p76]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P76 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]] 1.93&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=P76:N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-[4-(PHENYLETHYNYL)PHENYL]PIPERIDINE-1-CARBOXAMIDE'>P76</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3p76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p76 OCA], [https://pdbe.org/3p76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p76 RCSB], [https://www.ebi.ac.uk/pdbsum/3p76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p76 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LPXC_AQUAE LPXC_AQUAE] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibiotic resistant hospital acquired infections are on the rise, creating an urgent need for novel bactericidal drugs. Enzymes involved in lipopolysaccharide (LPS) biosynthesis are attractive antibacterial targets since LPS is the major structural component of the outer membrane of Gram-negative bacteria. Lipid A is an essential hydrophobic anchor of LPS and the first committed step in lipid A biosynthesis is catalyzed by a unique zinc dependent metalloamidase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC). LpxC is an attractive Gram-negative only target that has been chemically validated by potent bactericidal hydroxamate inhibitors that work by coordination of the enzyme's catalytic zinc ion. An exploratory chemistry effort focused on expanding the SAR around hydroxamic acid zinc-binding 'warheads' lead to the identification of novel compounds with enzyme potency and antibacterial activity similar to CHIR-090.

Design and synthesis of potent Gram-negative specific LpxC inhibitors.,Faruk Mansoor U, Vitharana D, Reddy PA, Daubaras DL, McNicholas P, Orth P, Black T, Arshad Siddiqui M Bioorg Med Chem Lett. 2011 Feb 15;21(4):1155-61. Epub 2010 Dec 28. PMID:21273067<ref>PMID:21273067</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3p76" style="background-color:#fffaf0;"></div>

==See Also==
*[[UDP-3-O-acyl-N-acetylglucosamine deacetylase|UDP-3-O-acyl-N-acetylglucosamine deacetylase]]
== References ==
<references/>
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</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Orth P]]