5zj0: Difference between revisions
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<StructureSection load='5zj0' size='340' side='right'caption='[[5zj0]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5zj0' size='340' side='right'caption='[[5zj0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zj0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJ0 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5zj0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZJ0 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]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zj0 OCA], [https://pdbe.org/5zj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zj0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zj0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A3E1L4S6_XANCA A0A3E1L4S6_XANCA] | |||
<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: Xanthomonas campestris]] | ||
[[Category: | [[Category: Hong HJ]] | ||
[[Category: | [[Category: Kim TH]] | ||
[[Category: | [[Category: Song WS]] | ||
[[Category: | [[Category: Yoon SI]] | ||
Revision as of 11:57, 22 November 2023
Crystal structure of Xanthomonas campestris FlgL (space group C2)Crystal structure of Xanthomonas campestris FlgL (space group C2)
Structural highlights
FunctionPublication Abstract from PubMedBacteria move toward attractants and away from repellants by rotating their flagellum. The bacterial flagellum assembles through the ordered organization of more than 30 different proteins. Among the diverse flagellar proteins, FlgL forms the junction between the hook and the filament in the flagellum together with FlgK and provides a structural base where flagellin, a filament-forming protein, is inserted for the initiation of filament elongation. However, the functional and structural information available for FlgL is highly limited. To provide structural insights into the cross-linkage between the FlgL junction and the flagellin filament, we determined the crystal structures of FlgL from gram-positive Bacillus cereus (bcFlgL) and gram-negative Xanthomonas campestris (xcFlgL). bcFlgL contains one domain (D1), whereas xcFlgL adopts a two-domain structure that consists of the D1 and D2 domains. The constant D1 domain of FlgL adopts a rod structure that is generated by four longitudinal segments. This four-segment structure is recapitulated in filament and junction proteins but not in hook and rod proteins, allowing us to propose a junction-filament assembly mechanism based on a quasi-homotypic interaction. The D2 domain of xcFlgL resembles that of another junction protein, FlgK, suggesting the structural and functional relatedness of FlgL and FlgK. Crystal structure of FlgL and its implications for flagellar assembly.,Hong HJ, Kim TH, Song WS, Ko HJ, Lee GS, Kang SG, Kim PH, Yoon SI Sci Rep. 2018 Sep 24;8(1):14307. doi: 10.1038/s41598-018-32460-9. PMID:30250171[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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