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3pmo

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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==
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<StructureSection load='3pmo' size='340' side='right' caption='[[3pmo]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='3pmo' size='340' side='right'caption='[[3pmo]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pmo]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PMO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpxD, PA3646 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<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>
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<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=3pmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pmo OCA], [http://pdbe.org/3pmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pmo RCSB], [http://www.ebi.ac.uk/pdbsum/3pmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pmo ProSAT]</span></td></tr>
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<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 ==
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[[http://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]
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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LpxD 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.
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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<ref>PMID:21795786</ref>
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==See Also==
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*[[UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3pmo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Badger, J]]
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[[Category: Large Structures]]
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[[Category: Chie-Leon, B]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Logan, C]]
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[[Category: Badger J]]
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[[Category: Nienaber, V]]
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[[Category: Chie-Leon B]]
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[[Category: Sankaran, B]]
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[[Category: Logan C]]
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[[Category: Sridhar, V]]
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[[Category: Nienaber V]]
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[[Category: Zwart, P H]]
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[[Category: Sankaran B]]
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[[Category: Lipid a biosynthesis pathway]]
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[[Category: Sridhar V]]
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[[Category: Transferase]]
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[[Category: Zwart PH]]

Current revision

The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution

PDB ID 3pmo

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