Infrared dichroism of twisted beta-sheet barrels. The structure of E. coli outer membrane proteins.

Abstract:

:The infrared dichroic ratios of the amide bands from oriented beta-barrels yield an experimental value for the mean orientation, beta, of the beta-strands, relative to the barrel axis. For a barrel of n strands, this then gives the shear number, S, that characterizes the stagger of the beta-sheet. Combining values of beta and n specifies the barrel geometry by using the optimized model of Murzin, Lesk & Chothia for regular barrels. Application to published infrared data on the Escherichia coli outer membrane protein, OmpA yields S=9-10 (n=8), a barrel radius of 0.81(+/-0.01) nm, and an internal free volume of 0.031 nm(3) per residue, where the average twist of the beta-sheets is theta approximately 28 degrees, and their coiling angle is epsilon approximately 1 degrees. Hydrophobic matching of the 2.6 nm transmembrane stretch partly determines the shear number of the OmpA beta-barrel.

journal_name

J Mol Biol

authors

Marsh D

doi

10.1006/jmbi.2000.3557

keywords:

subject

Has Abstract

pub_date

2000-03-31 00:00:00

pages

803-8

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)93557-5

journal_volume

297

pub_type

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