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Copyright © 1996 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 70, Issue 4, 1590-1602, 1 April 1996

doi:10.1016/S0006-3495(96)79745-X

Research Article


Active site comparisons highlight structural similarities between myosin and other P-loop proteins

C.A. Smith and I. Rayment

Institute for Enzyme Research, University of Wisconsin, Madison 53705, USA.


Abstract

The phosphate binding loop (P-loop) is a common feature of a large number of enzymes that bind nucleotide whose consensus sequence is often used as a fingerprint for identifying new members of this group. We review here the binding sites of nine purine nucleotide binding proteins, with a focus on their relationship to the active site of myosin. This demonstrates that there is considerable conversation in the distribution and nature of the ligands that coordinate the triphosphate moiety. This comparison further suggests that at least myosin and the G-proteins utilize a similar mechanism for nucleotide hydrolysis.