Thursday, July 8, 2010

Structural Mechanisms for Domain Movements in Proteins

Structural Mechanisms for Domain Movements in Proteins ...Q Copyright 1994 by the American Chemical Society Perspectives in Biochemistry -- Volume 33, Number 22 June 7, 1994 Structural Mechanisms for Domain Movements in Proteins? Mark Gerstein,'J$s Arthur M. Lesk,'.ll and Cyrus Chothia'v*vl MRC Laboratory of Molecular Biology. Department of Haematology, Cambridge University, and Cambridge Center for Protein Engineering, Hills Road, Cambridge CB2 ZQH, U.K. Received February 15, 1994; Revised Manuscript Received April I, 1994" ABSTRACT: We survey all the known instances of domain movements in proteins for which

there is crystallographic evidence for the movement. We explain these domain movements in terms of the repertoire of low-energy conformation changes that are known to occur in proteins. We first describe the basic elements of this repertoire, hinge and shear motions, and then show how the elements of the repertoire can be combined to produce domain movements. We emphasize that the elements used in particular proteins are determined mainly by the structure of the interfaces between the domains. Nearly all large proteins are built from domains (Wodak & Janin, 1981), and large relative movements of domains provide spectacular examples of protein flexibility. Domain motions are important for a variety of protein functions, including catalysis, regulation of activity, transport of me- tabolites, formation of protein assemblies, and cellular locomotion. Domains often close around a binding site between them. Generally, the presence of bound substrates stabilizes a closed conformation, and their absence favors an open conformation. Consequently, domain motions illustrate induced fit in protein recognition (Koshland, 1958). Most of our information on the mechanisms of domain movements has come from X-ray crystal structures of open and closed conformations of particular proteins. The results of early investigations were reviewed by Janin and Wodak...

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