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| | ==Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (LpxA) from Moraxella catarrhalis RH4.== | | ==Crystal structure of UDP-N-acetylglucosamine O-acyltransferase (LpxA) from Moraxella catarrhalis RH4.== |
| - | <StructureSection load='5jxx' size='340' side='right' caption='[[5jxx]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='5jxx' size='340' side='right'caption='[[5jxx]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jxx]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Morcb Morcb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JXX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jxx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_catarrhalis_BBH18 Moraxella catarrhalis BBH18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JXX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 3.001Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxA, MCR_0549 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1236608 MORCB])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=5jxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxx OCA], [https://pdbe.org/5jxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jxx RCSB], [https://www.ebi.ac.uk/pdbsum/5jxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxx 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=5jxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxx OCA], [http://pdbe.org/5jxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxx RCSB], [http://www.ebi.ac.uk/pdbsum/5jxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D5VAW8_MORCB D5VAW8_MORCB]] 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][SAAS:SAAS00720115] | + | [https://www.uniprot.org/uniprot/D5VAW8_MORCB D5VAW8_MORCB] 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][SAAS:SAAS00720115] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5jxx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5jxx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Morcb]] | + | [[Category: Large Structures]] |
| - | [[Category: Dev, A]] | + | [[Category: Moraxella catarrhalis BBH18]] |
| - | [[Category: Kesari, P]] | + | [[Category: Dev A]] |
| - | [[Category: Kumar, P]] | + | [[Category: Kesari P]] |
| - | [[Category: Narwal, M]] | + | [[Category: Kumar P]] |
| - | [[Category: Pratap, S]] | + | [[Category: Narwal M]] |
| - | [[Category: Yadav, R]] | + | [[Category: Pratap S]] |
| - | [[Category: Acyltransferase]]
| + | [[Category: Yadav R]] |
| - | [[Category: Lpxa]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp-n-acetylglucosamine o-acyltransferase]]
| + | |
| Structural highlights
Function
D5VAW8_MORCB 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][SAAS:SAAS00720115]
Publication Abstract from PubMed
Lipopolysaccharide (LPS) is an important surface component and a potential virulence factor in the pathogenesis of Gram-negative bacteria. UDP-N-acetylglucosamine acyltransferase (LpxA) enzyme catalyzes the first reaction of LPS biosynthesis, reversible transfer of R-3-hydroxy-acyl moiety from donor R-3-hydroxy-acyl-acyl carrier protein to the 3' hydroxyl position of UDP-N-acetyl-glucosamine. LpxA enzyme's essentiality in bacterial survival and absence of any homologous protein in humans makes it a promising target for anti-bacterial drug development. Herein, we present the crystal structure of Moraxella catarrhalis LpxA (McLpxA). We propose that L171 is responsible for limiting the acyl chain length in McLpxA to 10C or 12C. The study reveals the plausible interactions between the highly conserved clusters of basic residues at the C-terminal end of McLpxA and acidic residues of acyl carrier protein (ACP). Furthermore, the crystal structure of McLpxA was used to screen potential inhibitors from NCI open database using various computational approaches viz. pharmacophore mapping, virtual screening and molecular docking. Molecules Mol212032, Mol609399 and Mol152546 showed best binding affinity with McLpxA among all screened molecules. These molecules mimic the substrate-LpxA binding interactions.
Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA: Insight through crystal structure and computational studies.,Pratap S, Kesari P, Yadav R, Dev A, Narwal M, Kumar P Int J Biol Macromol. 2017 Mar;96:759-765. doi: 10.1016/j.ijbiomac.2017.01.005., Epub 2017 Jan 3. PMID:28057571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pratap S, Kesari P, Yadav R, Dev A, Narwal M, Kumar P. Acyl chain preference and inhibitor identification of Moraxella catarrhalis LpxA: Insight through crystal structure and computational studies. Int J Biol Macromol. 2017 Mar;96:759-765. doi: 10.1016/j.ijbiomac.2017.01.005., Epub 2017 Jan 3. PMID:28057571 doi:http://dx.doi.org/10.1016/j.ijbiomac.2017.01.005
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