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dc.contributor.author Deis, LN
dc.contributor.author Pemble, CW
dc.contributor.author Qi, Y
dc.contributor.author Hagarman, A
dc.contributor.author Richardson, DC
dc.contributor.author Richardson, JS
dc.contributor.author Oas, TG
dc.coverage.spatial United States
dc.date.accessioned 2015-12-15T15:25:20Z
dc.date.accessioned 2015-12-15T15:25:59Z
dc.date.issued 2014-10-07
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/25295398
dc.identifier S0969-2126(14)00278-0
dc.identifier.citation Structure, 2014, 22 (10), pp. 1467 - 1477
dc.identifier.uri http://hdl.handle.net/10161/11167
dc.description.abstract The Staphylococcus aureus virulence factor staphylococcal protein A (SpA) is a major contributor to bacterial evasion of the host immune system, through high-affinity binding to host proteins such as antibodies. SpA includes five small three-helix-bundle domains (E-D-A-B-C) separated by conserved flexible linkers. Prior attempts to crystallize individual domains in the absence of a binding partner have apparently been unsuccessful. There have also been no previous structures of tandem domains. Here we report the high-resolution crystal structures of a single C domain, and of two B domains connected by the conserved linker. Both structures exhibit extensive multiscale conformational heterogeneity, which required novel modeling protocols. Comparison of domain structures shows that helix1 orientation is especially heterogeneous, coordinated with changes in side chain conformational networks and contacting protein interfaces. This represents the kind of structural plasticity that could enable SpA to bind multiple partners.
dc.format.extent 1467 - 1477
dc.language eng
dc.relation.ispartof Structure
dc.relation.isversionof 10.1016/j.str.2014.08.014
dc.relation.replaces http://hdl.handle.net/10161/11166
dc.relation.replaces 10161/11166
dc.subject Crystallography, X-Ray
dc.subject Models, Molecular
dc.subject Protein Conformation
dc.subject Protein Structure, Tertiary
dc.subject Staphylococcal Protein A
dc.subject Staphylococcus aureus
dc.title Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.
dc.type Journal Article
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/25295398
pubs.issue 10
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Biochemistry
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.publication-status Published
pubs.volume 22
dc.identifier.eissn 1878-4186

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