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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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dc.contributor.author Kang, Hae Joo ko
dc.contributor.author Paterson, Neil G. ko
dc.contributor.author Kim, Chae Un ko
dc.contributor.author Middleditch, Martin ko
dc.contributor.author Chang, Chungyu ko
dc.contributor.author Ton-That, Hung ko
dc.contributor.author Baker, Edward N. ko
dc.date.available 2014-05-27T02:21:13Z -
dc.date.created 2014-05-27 ko
dc.date.issued 2014-05 ko
dc.identifier.citation ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.70, no.5, pp.1190 - 1201 ko
dc.identifier.issn 2059-7983 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/4786 -
dc.description.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. ko
dc.description.statementofresponsibility open -
dc.language 영어 ko
dc.publisher WILEY-BLACKWELL ko
dc.title A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-84900385997 ko
dc.identifier.wosid 000335952500002 ko
dc.type.rims ART ko
dc.description.wostc 0 *
dc.description.scopustc 0 *
dc.date.tcdate 2014-10-18 *
dc.date.scptcdate 2014-07-12 *
dc.identifier.doi 10.1107/S1399004714001400 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84900385997 ko
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