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dc.contributor.author Deis, LN
dc.contributor.author Hagarman, A
dc.contributor.author Oas, Terrence Gilbert
dc.contributor.author Pemble IV, Charles W
dc.contributor.author Qi, Y
dc.contributor.author Richardson, DC
dc.contributor.author Richardson, JS
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.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.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.begin-page 1467
pubs.end-page 1477
pubs.issue 10
pubs.organisational-group Basic Science Departments
pubs.organisational-group Biochemistry
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group School of Medicine
pubs.publication-status Published
pubs.volume 22
dc.identifier.eissn 1878-4186


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