Structural highlights
Function
[OMPA_ECOLI] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
High-resolution structure of the OmpA membrane domain.,Pautsch A, Schulz GE J Mol Biol. 2000 Apr 28;298(2):273-82. PMID:10764596[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pautsch A, Schulz GE. High-resolution structure of the OmpA membrane domain. J Mol Biol. 2000 Apr 28;298(2):273-82. PMID:10764596 doi:10.1006/jmbi.2000.3671
