Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis.

@article{citeulike:1049133, abstract = {The major feature of many proteins is a large beta-sheet that twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last: the beta-sheet barrel. McLachlan classified barrels in terms of two integral parameters: the number of strands in the beta-sheet, n, and the "shear number", S, a measure of the stagger of the strands in the beta-sheet. He showed that the mean radius of a barrel and the extent to which strands are tilted relative to its axis are determined by the values of n and S. Here we show that the (n, S) values determine all the other general structural features of regular beta-sheet barrels, in particular, optimal values of the twist and coiling angles that produce the closed beta-sheet, the hyperboloidal shape and the arrangement of residues in the barrel interior. Consideration of the residue arrangements in the interiors of different potential barrel structures, and of side-chain volumes, suggest that barrels, in which the interiors are close packed by the residues in beta-sheets with good geometries, have structures that correspond to one of only ten different combinations of n and S. In the accompanying paper, we demonstrate, by an analysis of all observed protein structures that contain beta-sheet barrels and for which atomic co-ordinates are available, the validity of these theoretical results.}, address = {MRC Laboratory of Molecular Biology, University of Cambridge Clinical School, U.K.}, author = {Murzin, A. G. and Lesk, A. M. and Chothia, C. }, citeulike-article-id = {1049133}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {barrel, jcsg, protein\_structure}, month = {March}, number = {5}, pages = {1369--1381}, posted-at = {2007-01-18 19:10:07}, priority = {4}, title = {Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8126726}, volume = {236}, year = {1994} }

TY - JOUR ID - citeulike:1049133 L3 - citeulike-article-id:1049133 TI - Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis. JF - J Mol Biol VL - 236 IS - 5 SP - 1369 EP - 1381 AD - MRC Laboratory of Molecular Biology, University of Cambridge Clinical School, U.K. SN - 0022-2836 N2 - The major feature of many proteins is a large beta-sheet that twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last: the beta-sheet barrel. McLachlan classified barrels in terms of two integral parameters: the number of strands in the beta-sheet, n, and the "shear number", S, a measure of the stagger of the strands in the beta-sheet. He showed that the mean radius of a barrel and the extent to which strands are tilted relative to its axis are determined by the values of n and S. Here we show that the (n, S) values determine all the other general structural features of regular beta-sheet barrels, in particular, optimal values of the twist and coiling angles that produce the closed beta-sheet, the hyperboloidal shape and the arrangement of residues in the barrel interior. Consideration of the residue arrangements in the interiors of different potential barrel structures, and of side-chain volumes, suggest that barrels, in which the interiors are close packed by the residues in beta-sheets with good geometries, have structures that correspond to one of only ten different combinations of n and S. In the accompanying paper, we demonstrate, by an analysis of all observed protein structures that contain beta-sheet barrels and for which atomic co-ordinates are available, the validity of these theoretical results. KW - barrel KW - jcsg KW - protein_structure AU - Murzin, AG AU - Lesk, AM AU - Chothia, C PY - 1994/03/11/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8126726 ER -