5iv8: Difference between revisions
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<StructureSection load='5iv8' size='340' side='right'caption='[[5iv8]], [[Resolution|resolution]] 2.94Å' scene=''> | <StructureSection load='5iv8' size='340' side='right'caption='[[5iv8]], [[Resolution|resolution]] 2.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5iv8]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5iv8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IV8 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]] 2.938Å</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=5iv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iv8 OCA], [https://pdbe.org/5iv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iv8 RCSB], [https://www.ebi.ac.uk/pdbsum/5iv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iv8 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/A0A0J4W1Y0_KLEVA A0A0J4W1Y0_KLEVA] Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.[HAMAP-Rule:MF_01186] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Klebsiella pneumoniae]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Botos | [[Category: Botos I]] | ||
[[Category: Buchanan | [[Category: Buchanan SK]] | ||
[[Category: McCarthy | [[Category: McCarthy JG]] | ||
Latest revision as of 13:33, 6 September 2023
The LPS Transporter LptDE from Klebsiella pneumoniae, core complexThe LPS Transporter LptDE from Klebsiella pneumoniae, core complex
Structural highlights
FunctionA0A0J4W1Y0_KLEVA Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.[HAMAP-Rule:MF_01186] 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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