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| | <StructureSection load='6hy2' size='340' side='right'caption='[[6hy2]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6hy2' size='340' side='right'caption='[[6hy2]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hy2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HY2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hy2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HY2 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxA, b0181, JW0176 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 1.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://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 [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </span></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=6hy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hy2 OCA], [https://pdbe.org/6hy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hy2 RCSB], [https://www.ebi.ac.uk/pdbsum/6hy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hy2 ProSAT]</span></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=6hy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hy2 OCA], [https://pdbe.org/6hy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hy2 RCSB], [https://www.ebi.ac.uk/pdbsum/6hy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hy2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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]
| + | [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] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the transfer of an R-3-hydroxyacyl chain from its acyl carrier protein (ACP) to the 3-OH group of UDP-GlcNAc. Essential in the growth of Gram-negative bacteria, LpxA is a logical target for antibiotics design. A pentadecapeptide (Peptide 920) with high affinity towards LpxA was previously identified in a phage display library. Here we created a small library of systematically designed peptides with the length of four to thirteen amino acids using Peptide 920 as a scaffold. The concentrations of these peptides at which 50% of LpxA is inhibited (IC50) range from 50 nM to >100 muM. We determined the crystal structure of E. coli LpxA in a complex with a potent inhibitor. LpxA-inhibitor interaction, solvent model and all contributing factors to inhibitor efficacy were well resolved. The peptide primarily occludes the ACP binding site of LpxA. Interactions between LpxA and the inhibitor are different from those in the structure of Peptide 920. The inhibitory peptide library and the crystal structure of inhibitor-bound LpxA described here may further assist in the rational design of inhibitors with antimicrobial activity that target LpxA and potentially other acyltransferases.
| + | |
| | | | |
| - | Structure guided design of an antibacterial peptide that targets UDP-N-acetylglucosamine acyltransferase.,Dangkulwanich M, Raetz CRH, Williams AH Sci Rep. 2019 Mar 8;9(1):3947. doi: 10.1038/s41598-019-40418-8. PMID:30850651<ref>PMID:30850651</ref>
| + | ==See Also== |
| - | | + | *[[UDP-N-acetylglucosamine acyltransferase 3D structures|UDP-N-acetylglucosamine acyltransferase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6hy2" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dangkulwanich, M]] | + | [[Category: Dangkulwanich M]] |
| - | [[Category: Williams, A H]] | + | [[Category: Williams AH]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Lpxa]]
| + | |
| - | [[Category: Transferase]]
| + | |
