2XGA

MTSL spin-labelled Shigella Flexneri Spa15

Summary for 2XGA

• Entry DOI: 10.2210/pdb2xga/pdb
• Related: 1RY9
• Descriptor: SURFACE PRESENTATION OF ANTIGENS PROTEIN SPAK, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate (3 entities in total)
• Functional Keywords: chaperone, virulence factor
• Biological source: SHIGELLA FLEXNERI
• Total number of polymer chains: 2
• Total formula weight: 35124.15

Authors

Lillington, J.E.D.,Johnson, S.,Lea, S.M. (deposition date: 2010-06-02, release date: 2010-12-01, Last modification date: 2024-11-20)

Primary citation

Lillington, J.E.D.,Lovett, J.E.,Johnson, S.,Roversi, P.,Timmel, C.R.,Lea, S.M.
Shigella Flexneri Spa15 Crystal Structure Verified in Solution by Double Electron Electron Resonance.
J.Mol.Biol., 405:427-, 2011

PubMed Abstract: Shigella flexneri Spa15 is a chaperone of the type 3 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 guanosine triphosphatase RhoG. In this study, Spa15 alone and in complex with IpgB1 has been studied by double electron electron resonance, an experiment that 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 double electron electron resonance 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.

PubMed: 21075116
DOI: 10.1016/J.JMB.2010.10.053

Experimental method

X-RAY DIFFRACTION (2.3 Å)