2jmm
From Proteopedia
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NMR solution structure of a minimal transmembrane beta-barrel platform protein
Overview
In this study, we were concerned with the structural role of the, surface-exposed extracellular loops of the N-terminal transmembrane (TM), domain of OmpA. A variant of the TM domain of outer membrane protein A, (OmpA) with all four such loops shortened, which we call the beta-barrel, platform (BBP), was successfully refolded. This indicates that the removed, parts of the surface-exposed loops indeed do not contain amino acid, sequences critical for this membrane protein's refolding in vitro. BBP has, the potential to be used as a template beta-barrel membrane protein, structure for the development of novel functions, although our results, also highlight the potential difficulties that can arise when, functionality is being engineered into the loop regions of membrane, proteins. We have used solution nuclear magnetic resonance spectroscopy to, determine the global fold of BBP+EF, BBP with a metal ion-binding EF-hand, inserted in one of the shortened loops. BBP and BBP+EF in, dihexanoylphosphatidylcholine micelles are eight-stranded antiparallel, beta-barrels, and BBP represents the smallest beta-structured integral, membrane protein known to date.
About this Structure
2JMM is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance., Johansson MU, Alioth S, Hu K, Walser R, Koebnik R, Pervushin K, Biochemistry. 2007 Feb 6;46(5):1128-40. PMID:17260943
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