Download The structure of components of a multi

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)