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Structure paper

TitleAn asymmetric sheath controls flagellar supercoiling and motility in the Leptospira spirochete.
Journal, issue, pagesElife, Vol. 9, Page e53672-, Year 2020
Publish dateJan 22, 2019 (structure data deposition date)
AuthorsGibson, K. / Trajtenberg, F. / Brady, M. / San Martin, F. / Mechaly, A. / Wunder, E. / Picardeau, M. / Ko, A. / Buschiazzo, A. / Sindelar, C.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.5 - 2.58 Å
Structure data

PDB-6nqy:
Flagellar protein FcpA from Leptospira biflexa / ab-centered monoclinic form
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6nqz:
Flagellar protein FcpB from Leptospira interrogans
Method: X-RAY DIFFRACTION / Resolution: 2.58 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-IOD:
IODIDE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-I3C:
5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid

Source
  • leptospira biflexa serovar patoc (strain patoc 1 / atcc 23582 / paris) (bacteria)
  • leptospira interrogans serogroup icterohaemorrhagiae serovar copenhageni (strain fiocruz l1-130) (bacteria)
KeywordsPROTEIN FIBRIL / flagellar filament

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