5fhy: Difference between revisions
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==Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1== | ==Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1== | ||
<StructureSection load='5fhy' size='340' side='right' caption='[[5fhy]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5fhy' size='340' side='right'caption='[[5fhy]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fhy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHY OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5fhy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FHY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliD, PA1094 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=5fhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhy OCA], [http://pdbe.org/5fhy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fhy RCSB], [http://www.ebi.ac.uk/pdbsum/5fhy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhy ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5fhy" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5fhy" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Flagellar proteins|Flagellar proteins]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pseae]] | |||
[[Category: Bonsor, D]] | [[Category: Bonsor, D]] | ||
[[Category: Diederichs, K]] | [[Category: Diederichs, K]] | ||
Revision as of 10:20, 6 May 2020
Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1
Structural highlights
Function[FLID2_PSEAE] Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential for motility. Responsible for adhesion to mucin, which is the initial event in colonization by this organism of the airways of cystic fibrosis patients. Publication Abstract from PubMedFlagella are critical for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed resulting in impaired motility and infectivity. Here, we report the 2.2 A resolution X-ray crystal structure of FliD from Pseudomonas aeruginosa, the first high-resolution structure of any FliD protein from any bacterium. In combination with a multitude of biophysical and functional analyses, we find that Pseudomonas FliD exhibits unexpected structural similarity to other flagellar proteins at the domain level, adopts a unique hexameric oligomeric state, and depends on flexible determinants for oligomerization. Considering that the flagellin filaments on which FliD oligomers are affixed vary between bacteria in protofilament number, our results suggest that FliD oligomer stoichiometries vary across bacteria to complement their filament assemblies. Bacterial flagellar capping proteins adopt diverse oligomeric states.,Postel S, Deredge D, Bonsor DA, Yu X, Diederichs K, Helmsing S, Vromen A, Friedler A, Hust M, Egelman EH, Beckett D, Wintrode PL, Sundberg EJ Elife. 2016 Sep 24;5. pii: e18857. doi: 10.7554/eLife.18857. PMID:27664419[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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