This Article Full Text Full Text (PDF) Supplemental All Versions of this Article: biophysj.106.097311v1 92/2/L23    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bond, P. J. Articles by Sansom, M. S. P. Search for Related Content PubMed PubMed Citation Articles by Bond, P. J. Articles by Sansom, M. S. P.

Membrane Simulations of OpcA: Gating in the Loops?

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

^* Department of Biochemistry, University of Oxford, Oxford, United Kingdom; and Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom

Correspondence: Address reprint requests and inquiries to Mark S. P. Sansom, Tel.: 44-1865-275371; Fax: 44-1865-275273; E-mail: mark.sansom{at}bioch.ox.ac.uk.

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 Neisseria 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 nonphysiological state. The presence of lipids and physiological salt concentrations result in changes in the conformation of the extracellular loops of OpcA, leading to opening of a 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.

This article has been cited by other articles:

				G. Duret, M. Szymanski, K.-J. Choi, H.-J. Yeo, and A. H. Delcour The TpsB Translocator HMW1B of Haemophilus influenzae Forms a Large Conductance Channel J. Biol. Chem., June 6, 2008; 283(23): 15771 - 15778. [Abstract] [Full Text] [PDF]

				B. Luan, M. Caffrey, and A. Aksimentiev Structure Refinement of the OpcA Adhesin Using Molecular Dynamics Biophys. J., November 1, 2007; 93(9): 3058 - 3069. [Abstract] [Full Text] [PDF]