3pmo: Difference between revisions
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==The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution== | ==The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution== | ||
<StructureSection load='3pmo' size='340' side='right' caption='[[3pmo]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='3pmo' size='340' side='right'caption='[[3pmo]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pmo]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PMO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxD, PA3646 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxD, PA3646 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pmo OCA], [https://pdbe.org/3pmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pmo RCSB], [https://www.ebi.ac.uk/pdbsum/3pmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pmo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/LPXD_PSEAE LPXD_PSEAE]] Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-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.[HAMAP-Rule:MF_00523] | ||
<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 3pmo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3pmo" 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: Large Structures]] | |||
[[Category: Badger, J]] | [[Category: Badger, J]] | ||
[[Category: Chie-Leon, B]] | [[Category: Chie-Leon, B]] | ||
Revision as of 11:46, 25 May 2022
The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolutionThe structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution
Structural highlights
Function[LPXD_PSEAE] Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-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.[HAMAP-Rule:MF_00523] Publication Abstract from PubMedLpxD is a bacterial protein that is part of the biosynthesis pathway of lipid A and is responsible for transferring 3-hydroxymyristic acid from the R-3-hydroxymyristoyl-acyl carrier protein to the 2-OH group of UDP-3-O-(3-hydroxymyristoyl) glucosamine. The crystal structure of LpxD from Pseudomonas aeruginosa has been determined at high resolution (1.3 A). The crystal belonged to space group H3, with unit-cell parameters a=b=106.19, c=93.38 A, and contained one molecule in the asymmetric unit. The structure was solved by molecular replacement using the known structure of LpxD from Escherichia coli (PDB entry 3eh0) as a search model and was refined to Rwork=16.4% (Rfree=18.5%) using 91,655 reflections. The final protein model includes 355 amino-acid residues (including 16 amino acids from a 20 amino-acid N-terminal His tag), one chloride ion and two ethylene glycol molecules. The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution.,Badger J, Chie-Leon B, Logan C, Sridhar V, Sankaran B, Zwart PH, Nienaber V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):749-52., Epub 2011 Jun 23. PMID:21795786[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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