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TitleA slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1190-1201, Year 2014
Publish dateOct 30, 2012 (structure data deposition date)
AuthorsKang, H.J. / Paterson, N.G. / Kim, C.U. / Middleditch, M. / Chang, C. / Ton-That, H. / Baker, E.N.
External linksActa Crystallogr. ,Sect. D / PubMed:24816089
MethodsX-ray diffraction
Resolution1.87 - 2.5 Å
Structure data

PDB-4hsq:
Crystal Structure of Domains D2 and D3 of the Major Pilin SpaD from Corynebacterium diphtheriae
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-4hss:
Structure of the Full-Length Major Pilin SpaD from Corynebacterium diphtheriae
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • corynebacterium diphtheriae (bacteria)
KeywordsCELL ADHESION / CnaA/CnaB domains / Major Pilin / Isopeptide bond via Lys-Asn side chains / CnaA/CnaB folded domains / Major pilin polymer / Homopolymer / Isopeptide bonding between Lys and Asn sidechains

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