1l0m
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(New page: 200px<br /><applet load="1l0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0m" /> '''Solution structure of Bacteriorhodopsin'''<b...)
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Revision as of 18:01, 20 November 2007
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Solution structure of Bacteriorhodopsin
Overview
Three-dimensional structures of only a handful of membrane proteins have, been solved, in contrast to the thousands of structures of water-soluble, proteins. Difficulties in crystallization have inhibited the determination, of the three-dimensional structure of membrane proteins by x-ray, crystallography and have spotlighted the critical need for alternative, approaches to membrane protein structure. A new approach to the, three-dimensional structure of membrane proteins has been developed and, tested on the integral membrane protein, bacteriorhodopsin, the crystal, structure of which had previously been determined. An overlapping series, of 13 peptides, spanning the entire sequence of bacteriorhodopsin, was, synthesized, and the structures of these peptides were determined by NMR, in dimethylsulfoxide solution. These structures were assembled into a, three-dimensional construct by superimposing the overlapping sequences at, the ends of each peptide. Onto this construct were written all the, distance and angle constraints obtained from the individual solution, structures along with a limited number of experimental inter-helical, distance constraints, and the construct was subjected to simulated, annealing. A three-dimensional structure, determined exclusively by the, experimental constraints, emerged that was similar to the crystal, structure of this protein. This result suggests an alternative approach to, the acquisition of structural information for membrane proteins consisting, of helical bundles.
About this Structure
1L0M is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin., Katragadda M, Alderfer JL, Yeagle PL, Biophys J. 2001 Aug;81(2):1029-36. PMID:11463644
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