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Kim, Chae Un
High Pressure X-ray Science Lab (HiPreX)
Research Interests
  • X-ray Science, biophysical science, biomedical science

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A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly

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Title
A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly
Author
Kang, Hae JooPaterson, Neil G.Kim, Chae UnMiddleditch, MartinChang, ChungyuTon-That, HungBaker, Edward N.
Keywords
Gram-positive bacterial pili; isopeptide bond; pilus assembly
Issue Date
201405
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.70, no.5, pp.1190 - 1201
Abstract
The Gram-positive organism Corynebacterium diphtheriae, the cause of diphtheria in humans, expresses pili on its surface which it uses for adhesion and colonization of its host. These pili are covalent protein polymers composed of three types of pilin subunit that are assembled by specific sortase enzymes. A structural analysis of the major pilin SpaD, which forms the polymeric backbone of one of the three types of pilus expressed by C. diphtheriae, is reported. Mass-spectral and crystallographic analysis shows that SpaD contains three internal Lys-Asn isopeptide bonds. One of these, shown by mass spectrometry to be located in the N-terminal D1 domain of the protein, only forms slowly, implying an energy barrier to bond formation. Two crystal structures, of the full-length three-domain protein at 2.5Å resolution and of a two-domain (D2-D3) construct at 1.87Å resolution, show that each of the three Ig-like domains contains a single Lys-Asn isopeptide-bond cross-link, assumed to give mechanical stability as in other such pili. Additional stabilizing features include a disulfide bond in the D3 domain and a calcium-binding loop in D2. The N-terminal D1 domain is more flexible than the others and, by analogy with other major pilins of this type, the slow formation of its isopeptide bond can be attributed to its location adjacent to the lysine used in sortase-mediated polymerization during pilus assembly.
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DOI
http://dx.doi.org/10.1107/S1399004714001400
ISSN
2059-7983
Appears in Collections:
SNS_Journal Papers
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