5ixm: Difference between revisions
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<StructureSection load='5ixm' size='340' side='right'caption='[[5ixm]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='5ixm' size='340' side='right'caption='[[5ixm]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ixm]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ixm]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IXM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.746Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ixm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ixm OCA], [https://pdbe.org/5ixm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ixm RCSB], [https://www.ebi.ac.uk/pdbsum/5ixm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ixm ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LPTD_YERPE LPTD_YERPE] Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.[HAMAP-Rule:MF_01411] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Yersinia pestis]] | ||
[[Category: | [[Category: Botos I]] | ||
[[Category: | [[Category: Buchanan SK]] | ||
[[Category: | [[Category: Mayclin SJ]] | ||
[[Category: | [[Category: McCarthy JG]] | ||
Revision as of 13:37, 6 September 2023
The LPS Transporter LptDE from Yersinia pestis, core complexThe LPS Transporter LptDE from Yersinia pestis, core complex
Structural highlights
FunctionLPTD_YERPE Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.[HAMAP-Rule:MF_01411] Publication Abstract from PubMedIncorporation of lipopolysaccharide (LPS) into the outer membrane of Gram-negative bacteria is essential for viability, and is accomplished by a two-protein complex called LptDE. We solved crystal structures of the core LptDE complexes from Yersinia pestis, Klebsiella pneumoniae, Pseudomonas aeruginosa, and a full-length structure of the K. pneumoniae LptDE complex. Our structures adopt the same plug and 26-strand beta-barrel architecture found recently for the Shigella flexneri and Salmonella typhimurium LptDE structures, illustrating a conserved fold across the family. A comparison of the only two full-length structures, SfLptDE and our KpLptDE, reveals a 21 degrees rotation of the LptD N-terminal domain that may impart flexibility on the trans-envelope LptCAD scaffold. Utilizing mutagenesis coupled to an in vivo functional assay and molecular dynamics simulations, we demonstrate the critical role of Pro231 and Pro246 in the function of the LptD lateral gate that allows partitioning of LPS into the outer membrane. Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.,Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, Buchanan SK Structure. 2016 May 3. pii: S0969-2126(16)30043-0. doi:, 10.1016/j.str.2016.03.026. PMID:27161977[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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