* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download The structure of components of a multi
Membrane potential wikipedia , lookup
P-type ATPase wikipedia , lookup
Cell nucleus wikipedia , lookup
Model lipid bilayer wikipedia , lookup
Protein phosphorylation wikipedia , lookup
Theories of general anaesthetic action wikipedia , lookup
G protein–coupled receptor wikipedia , lookup
Magnesium transporter wikipedia , lookup
Homology modeling wikipedia , lookup
Protein moonlighting wikipedia , lookup
Signal transduction wikipedia , lookup
SNARE (protein) wikipedia , lookup
Cell membrane wikipedia , lookup
Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup
Protein structure prediction wikipedia , lookup
Proteolysis wikipedia , lookup
Trimeric autotransporter adhesin wikipedia , lookup
List of types of proteins wikipedia , lookup
Intrinsically disordered proteins wikipedia , lookup
13.20 The structure of components of a multi-component integral membrane pump of the HME RND family Robert Stroud1, John Pak1, Chantal Eckende1, John Lee1, Joseph D. O'Connell III1, Fabien DeAngelis2, Cedric Bauvois2, Cedric Govaerts2, Jean-Marie Ruysschaert2, Guy Vandenbussche2 1 UCSF, 2Université Libre de Bruxelles The focus of the talk will be on recent results that pertain to the structure of the components, and mechanisms of a protein in the heavy metal extrusion class of RND family, as compared with other proteins in this family (1) by X-ray diffraction and hybrid methods. We seek to understand the mechanisms of transmembrane transport and insight from the structures will be discussed. This involves crystallization of membrane proteins. Methods used to crystallize other transporters will be discussed as they pertain to new prospective methods for membrane proteins (2-5). Supported by National Institute of Health Grant RO1 GM24485, GM73210 and GM94625 1. De Angelis F, et al.. Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc Natl Acad Sci USA 107,11038-43. (2010) (PMID: 20534468 / PMCID: PMC2890744) 2. Egea PF, Stroud RM. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci USA. 40, 17182-7, (2010). (PMID: 20855604) 3. Chaudhary S, Pak JE, Pedersen BP, Bang LJ, Zhang LB, Ngaw SM, et al. Efficient expression screening of human membrane proteins in transiently transfected Human Embryonic Kidney 293S cells. Methods. (2011). 4. Gruswitz, F., et al. Function of human Rh based on structure of RhCG at 2.1 A Proc Natl Acad Sci U S A 107, 9638-9643 (2010) 5. Ho, J. D., et al. Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance. Proc Natl Acad Sci U S A 106, 7437-7442 (2009)