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Biophys. J. BioFAST: First Published November 17, 2006. doi:10.1529/biophysj.106.097311
© 2006 by the Biophysical Society.

A more recent version of this article appeared on January 15, 2007.
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MEMBRANES

Membrane Simulations of OpcA: Gating in the Loops?

Peter J. Bond 1, Jeremy P. Derrick 2 and Mark S.P. Sansom 1*

1 University of Oxford
2 University of Manchester

* To whom correspondence should be addressed. E-mail: mark.sansom{at}bioch.ox.ac.uk.

Submitted on September 13, 2006
Revised on September 30, 2006
Accepted on 7 November 2006


  Abstract
Mobility of extracellular loops may play an important role in the function of outer membrane proteins from Gram negative bacteria. Molecular dynamics simulations of OpcA from N.meningitidis, embedded in a lipid bilayer, have been used to explore the relationship between the crystal structure and dynamic function of this protein. The results suggest that the crystal environment may constrain the membrane protein structure in a non-physiological state. The presence of bilayer lipids and physiological salt concentrations result in changes in the conformation of the extracellular loops of OpcA, leading to opening of a possible pore, and to modulation of the molecular surface implicated in recognition of proteoglycan. These changes may be related to the role of OpcA in pathogenesis via modulation of the conformation of a possible sialic acid binding site.

Key Words: N. meningitidis, molecular dynamics, outer membrane protein, pore, sialic acid binding




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Copyright © 2006 by the Biophysical Society.