4zzf: Difference between revisions
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<StructureSection load='4zzf' size='340' side='right'caption='[[4zzf]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='4zzf' size='340' side='right'caption='[[4zzf]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zzf]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4zzf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZZF 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]] 2.1673Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zzf OCA], [https://pdbe.org/4zzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zzf RCSB], [https://www.ebi.ac.uk/pdbsum/4zzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zzf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/O25565_HELPY O25565_HELPY] Required for flagellar hook formation. May act as a scaffolding protein.[RuleBase:RU362076] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4zzf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4zzf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori 26695]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cendron | [[Category: Cendron L]] | ||
[[Category: Matkovic-Calogovic | [[Category: Matkovic-Calogovic D]] | ||
[[Category: Pulic | [[Category: Pulic I]] | ||
[[Category: Salamina | [[Category: Salamina M]] | ||
[[Category: Zanotti | [[Category: Zanotti G]] | ||
Latest revision as of 14:34, 9 May 2024
Crystal structure of truncated FlgD (tetragonal form) from the human pathogen Helicobacter pyloriCrystal structure of truncated FlgD (tetragonal form) from the human pathogen Helicobacter pylori
Structural highlights
FunctionO25565_HELPY Required for flagellar hook formation. May act as a scaffolding protein.[RuleBase:RU362076] Publication Abstract from PubMedFlagellin component D (FlgD) participates in the assembly of flagella, helical tubular structures that provide motility in non-filamentous bacteria. FlgD guides and controls the polymerization of FlgE that builds the hook, a short curved and hollow cylinder that connects the flagellar basal body spanning the cell envelope to the protruding filament. Crystal structures of truncated forms of Helicobacter pylori FlgD from two different strains in two space groups, I422 and P2, are reported here, at 2.2A and 2.8A resolution, respectively. Analogously to Pseudomonas aeruginosa and Xanthomonas campestris FlgD proteins, crystallization experiments set up for the full length protein resulted in crystals of a truncated form, lacking both N- and C-terminus ends. The crystal structures of the central domain show that the monomer is composed of a tudor and a fibronectin type III domain. The full length HpFlgD contains a long N-terminal signal region, probably partially flexible, a central globular region and a C-terminal segment with a peculiar repetitive pattern of amino acids. The spatial orientation of the two domains in HpFlgD differs from that of the homologous FlgD family members, P. aeruginosa and X. campestris. This difference together with the observation that HpFlgD assembles into tetramers, both in the solution and in the two crystal forms, strongly suggests that significant differences exist in the molecular organization of the flagella in different bacterial species. Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori.,Pulic I, Cendron L, Salamina M, Polverino de Laureto P, Matkovic-Calogovic D, Zanotti G J Struct Biol. 2016 Feb 8. pii: S1047-8477(16)30018-1. doi:, 10.1016/j.jsb.2016.02.003. PMID:26868107[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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