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Shigella flexneri Spa15 Crystal Structure Verified in solution by Double Electron Electron Resonance

DOI: 10.1016/j.jmb.2010.10.053 DOI Help
PMID: 21075116 PMID Help

Authors: James Lillington (University of Oxford) , Janet E. Lovett (Sir William Dunn School of Pathology, University of Oxford) , Steven Johnson (University of Oxford) , Pietro Roversi (University of Oxford) , Christine Timmel (University of Oxford) , Susan Lea (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Molecular Biology

State: Published (Approved)
Published: November 2010

Open Access Open Access

Abstract: Shigella flexneri Spa15 is a chaperone of the type three secretion system which binds a number of effectors to ensure their stabilization prior to secretion. One of these effectors is IpgB1, a mimic of the human Ras-like Rho GTPase RhoG. In this study, Spa15 alone and in complex with IpgB1 has been studied by double electron electron resonance (DEER), an experiment which gives distance information showing the spacial separation of attached spin labels. This distance is explained by determining the crystal structure of the spin labeled Spa15 where labels are seen to be buried in hydrophobic pockets. The DEER experiment on the Spa15 complex with IpgB1 shows that IpgB1 does not bind Spa15 in the same way as is seen in the homologous Salmonella sp. chaperone:effector complex InvB:SipA.

Journal Keywords: Crystallography; X-Ray; Electron; Electrons; Models; Molecular; Protein; Shigella; Solutions; Spin; rac1 GTP-Binding Protein

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

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