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| | <StructureSection load='2iu8' size='340' side='right'caption='[[2iu8]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2iu8' size='340' side='right'caption='[[2iu8]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iu8]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IU8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iu8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IU8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iu9|2iu9]], [[2iua|2iua]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu8 OCA], [http://pdbe.org/2iu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iu8 RCSB], [http://www.ebi.ac.uk/pdbsum/2iu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu8 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=2iu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu8 OCA], [https://pdbe.org/2iu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iu8 RCSB], [https://www.ebi.ac.uk/pdbsum/2iu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LPXD_CHLTR LPXD_CHLTR] Catalyzes the N-acylation of UDP-3-O-myristoylglucosamine using 3-hydroxyarachidoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (Probable).<ref>PMID:10358025</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2iu8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2iu8" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Chlamydia trachomatis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buetow, L]] | + | [[Category: Buetow L]] |
| - | [[Category: Dawson, A]] | + | [[Category: Dawson A]] |
| - | [[Category: Fyffe, S]] | + | [[Category: Fyffe S]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Smith, T K]] | + | [[Category: Smith TK]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Complex with udpglcnac]]
| + | |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Homotrimer]]
| + | |
| - | [[Category: Left-handed beta helix]]
| + | |
| - | [[Category: Lipid a biosynthesis]]
| + | |
| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp-3- o-acyl-glucosamine n-acyltransferase]]
| + | |
| Structural highlights
2iu8 is a 3 chain structure with sequence from Chlamydia trachomatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LPXD_CHLTR Catalyzes the N-acylation of UDP-3-O-myristoylglucosamine using 3-hydroxyarachidoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (Probable).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable LPS. The biosynthesis of LPS relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine in Chlamydia trachomatis. Our crystallographic study reveals that LpxD is a homotrimer, each subunit of which is constructed from a novel combination of an N-terminal uridine-binding domain, a core lipid-binding domain, and a C-terminal helical extension. Highly conserved residues dominate nucleotide binding. Phe-43 and Tyr-49 form pi-stacking interactions with uracil, and Asn-46 and His-284 form hydrogen bonds with the phosphate groups. These interactions place the glucosamine moiety at the catalytic center formed by two adjacent subunits. Here His-247 and His-284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate. Serendipitously, our study reveals a fatty acid (FA) binding groove near the catalytic center. MS elucidated the presence of a FA mixture binding to LpxD, with palmitic acid the most prevalent. The placement of UDP-N-acetylglucosamine and the FA provides details of N-acyltransferase ligand interactions and allows for a description of structure and reactivity at an early stage of LPS assembly.
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.,Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4321-6. Epub 2007 Mar 5. PMID:17360522[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rund S, Lindner B, Brade H, Holst O. Structural analysis of the lipopolysaccharide from Chlamydia trachomatis serotype L2. J Biol Chem. 1999 Jun 11;274(24):16819-24. PMID:10358025 doi:10.1074/jbc.274.24.16819
- ↑ Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4321-6. Epub 2007 Mar 5. PMID:17360522
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