4lcf: Difference between revisions

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 ==Crystal structure of the Pseudomonas aeruginosa LPXC/LPC-014 complex==
-<StructureSection load='4lcf' size='340' side='right' caption='[[4lcf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='4lcf' size='340' side='right'caption='[[4lcf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lcf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LCF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4lcf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LCF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WL:NALPHA-{4-[4-(4-AMINOPHENYL)BUTA-1,3-DIYN-1-YL]BENZOYL}-N-HYDROXY-L-HISTIDINAMIDE'>1WL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.599&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lcg|4lcg]], [[4lch|4lch]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WL:NALPHA-{4-[4-(4-AMINOPHENYL)BUTA-1,3-DIYN-1-YL]BENZOYL}-N-HYDROXY-L-HISTIDINAMIDE'>1WL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">envA, lpxC, PA4406 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=4lcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lcf OCA], [https://pdbe.org/4lcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lcf RCSB], [https://www.ebi.ac.uk/pdbsum/4lcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lcf ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lcf OCA], [http://pdbe.org/4lcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lcf RCSB], [http://www.ebi.ac.uk/pdbsum/4lcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lcf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LPXC_PSEAE LPXC_PSEAE]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
+[https://www.uniprot.org/uniprot/LPXC_PSEAE LPXC_PSEAE] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The zinc-dependent deacetylase LpxC catalyzes the committed step of lipid A biosynthesis in Gram-negative bacteria and is a validated target for development of novel antibiotics to combat multidrug-resistant Gram-negative infections. Many potent LpxC inhibitors contain an essential threonyl-hydroxamate head group for high-affinity interaction with LpxC. We report the synthesis, antibiotic activity, and structural and enzymatic characterization of novel LpxC inhibitors containing an additional aryl-group in the threonyl-hydroxamate moiety, which expands the inhibitor-binding surface in LpxC. These compounds display enhanced potency against LpxC in enzymatic assays and superior antibiotic activity against F. novicida in cell culture. Comparison of the antibiotic activities of these compounds against a leaky E. coli strain and the wild-type strain reveals the contribution of the formidable outer membrane permeability barrier that reduces the compound efficacy in cell culture and emphasizes the importance of maintaining a balanced hydrophobicity and hydrophilicity profile in developing effective LpxC-targeting antibiotics.
-Synthesis, structure and antibiotic activity of aryl-substituted LpxC inhibitors.,Liang X, Lee CJ, Zhao J, Toone EJ, Zhou P J Med Chem. 2013 Aug 5. PMID:23914798<ref>PMID:23914798</ref>
+==See Also==
+*[[UDP-3-O-acyl-N-acetylglucosamine deacetylase|UDP-3-O-acyl-N-acetylglucosamine deacetylase]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4lcf" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Pseae]]
+[[Category: Large Structures]]
-[[Category: Lee, C J]]
+[[Category: Pseudomonas aeruginosa PAO1]]
-[[Category: Zhou, P]]
+[[Category: Lee C-J]]
-[[Category: Acyl udp-glcnac]]
+[[Category: Zhou P]]
-[[Category: Baab sandwich]]
-[[Category: Deacetylation]]
-[[Category: Hydrolase-antibiotic complex]]
-[[Category: Hydroxamate]]
-[[Category: Lipid a biosynthesis]]
-[[Category: Lipid a synthesis]]
-[[Category: Lpxc]]