6pwb
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging== | |
+ | <StructureSection load='6pwb' size='340' side='right'caption='[[6pwb]], [[Resolution|resolution]] 9.83Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6pwb]] is a 163 chain structure with sequence from [http://en.wikipedia.org/wiki/Leptospira_biflexa_serovar_patoc_(strain_patoc_1_/_atcc_23582_/_paris) Leptospira biflexa serovar patoc (strain patoc 1 / atcc 23582 / paris)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PWB FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wjt|5wjt]], [[6nqz|6nqz]], [[6nqw|6nqw]], [[6nqx|6nqx]], [[6nqy|6nqy]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwb OCA], [http://pdbe.org/6pwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pwb RCSB], [http://www.ebi.ac.uk/pdbsum/6pwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/B0SSZ5_LEPBP B0SSZ5_LEPBP]] Component of the core of the flagella.[RuleBase:RU362073] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Spirochete bacteria, including important pathogens, exhibit a distinctive means of swimming via undulations of the entire cell. Motility is powered by the rotation of supercoiled 'endoflagella' that wrap around the cell body, confined within the periplasmic space. To investigate the structural basis of flagellar supercoiling, which is critical for motility, we determined the structure of native flagellar filaments from the spirochete Leptospira by integrating high-resolution cryo-electron tomography and X-ray crystallography. We show that these filaments are coated by a highly asymmetric, multi-component sheath layer, contrasting with flagellin-only homopolymers previously observed in exoflagellated bacteria. Distinct sheath proteins localize to the filament inner and outer curvatures to define the supercoiling geometry, explaining a key functional attribute of this spirochete flagellum. | ||
- | + | An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete.,Gibson KH, Trajtenberg F, Wunder EA, Brady MR, San Martin F, Mechaly A, Shang Z, Liu J, Picardeau M, Ko A, Buschiazzo A, Sindelar CV Elife. 2020 Mar 11;9. pii: 53672. doi: 10.7554/eLife.53672. PMID:32157997<ref>PMID:32157997</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 6pwb" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | [[Category: | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Buschiazzo, A]] | [[Category: Buschiazzo, A]] | ||
+ | [[Category: Gibson, K H]] | ||
+ | [[Category: Martin, F San]] | ||
+ | [[Category: Mechaly, A]] | ||
+ | [[Category: Sindelar, C V]] | ||
[[Category: Trajtenberg, F]] | [[Category: Trajtenberg, F]] | ||
+ | [[Category: Bacterial flagella]] | ||
+ | [[Category: Fcpa]] | ||
+ | [[Category: Fcpb]] | ||
+ | [[Category: Flaa]] | ||
+ | [[Category: Flab]] | ||
+ | [[Category: Leptospira]] | ||
+ | [[Category: Structural protein]] |
Revision as of 10:14, 27 March 2020
Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging
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Categories: Large Structures | Buschiazzo, A | Gibson, K H | Martin, F San | Mechaly, A | Sindelar, C V | Trajtenberg, F | Bacterial flagella | Fcpa | Fcpb | Flaa | Flab | Leptospira | Structural protein