1qjp
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(New page: 200px<br /><applet load="1qjp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qjp, resolution 1.65Å" /> '''HIGH RESOLUTION STRU...)
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Revision as of 22:38, 20 November 2007
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HIGH RESOLUTION STRUCTURE OF THE OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN
Overview
The membrane domain of OmpA consists of an eight-stranded, all-next-neighbor antiparallel beta-barrel with short turns at the, periplasmic barrel end and long flexible loops at the external end. The, structure analysis has been extended from medium resolution to 1. 65 A (1, A=0.1 nm), and the molecular model has been refined anisotropically to, show oriented mobilities of the structural elements. The improved data, allowed us to locate five further detergent molecules and 11 more water, molecules. Moreover, the two large non-polar packing contacts have now, been defined in detail. The analysis indicates that the beta-barrel, constitutes a solid scaffold such that the long external loops need not, contribute to stability. These loops are highly mobile and thus cause a, major problem during the crystallization process. The beta-barrel was, related to those of lipocalins. Two further crystal forms with, exceptionally dense packing arrangements were established at medium, resolution.
About this Structure
1QJP is a Single protein structure of sequence from Escherichia coli with C8E as ligand. Full crystallographic information is available from OCA.
Reference
High-resolution structure of the OmpA membrane domain., Pautsch A, Schulz GE, J Mol Biol. 2000 Apr 28;298(2):273-82. PMID:10764596
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