|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4r37' size='340' side='right'caption='[[4r37]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4r37' size='340' side='right'caption='[[4r37]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacfn Bacfn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis_NCTC_9343 Bacteroides fragilis NCTC 9343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R37 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r36|4r36]]</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=4r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r37 OCA], [https://pdbe.org/4r37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r37 RCSB], [https://www.ebi.ac.uk/pdbsum/4r37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r37 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxA, BF9343_0789 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272559 BACFN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r37 OCA], [http://pdbe.org/4r37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r37 RCSB], [http://www.ebi.ac.uk/pdbsum/4r37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r37 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q5LH16_BACFN Q5LH16_BACFN]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00064151] | + | [https://www.uniprot.org/uniprot/Q5LH16_BACFN Q5LH16_BACFN] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00064151] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacfn]] | + | [[Category: Bacteroides fragilis NCTC 9343]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, X]] | + | [[Category: Chen X]] |
| - | [[Category: Fisher, A J]] | + | [[Category: Fisher AJ]] |
| - | [[Category: Ngo, A]] | + | [[Category: Ngo A]] |
| - | [[Category: Left-handed beta helix]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp-n-acetylglucosamine acyltransferase]]
| + | |
| Structural highlights
Function
Q5LH16_BACFN Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00064151]
Publication Abstract from PubMed
Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. Lipid A constitutes a major component of lipopolysaccharides, also referred to as endotoxins, which form the outer monolayer of the outer membrane of Gram-negative bacteria. Ligand-free and UDP-GlcNAc-bound crystal structures of LpxA from Bacteroides fragilis NCTC 9343, the most common pathogenic bacteria found in abdominal abscesses, have been determined and are presented here. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-rung left-handed beta-helical (LbetaH) fold in the N-terminus followed by an alpha-helical motif in the C-terminus. The structure is highly similar to LpxA from other organisms. Yet, despite sharing a similar LbetaH structure with LpxAs from Escherichia coli and others, previously unseen calcium ions are observed on the threefold axis in B. fragilis LpxA to help stabilize the trimeric assembly.
Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA).,Ngo A, Fong KT, Cox DL, Chen X, Fisher AJ Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1068-76. doi:, 10.1107/S1399004715003326. Epub 2015 Apr 24. PMID:25945572[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ngo A, Fong KT, Cox DL, Chen X, Fisher AJ. Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA). Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1068-76. doi:, 10.1107/S1399004715003326. Epub 2015 Apr 24. PMID:25945572 doi:http://dx.doi.org/10.1107/S1399004715003326
|
