2JMM

NMR solution structure of a minimal transmembrane beta-barrel platform protein

Summary for 2JMM

• Entry DOI: 10.2210/pdb2jmm/pdb
• NMR Information: BMRB: 15045
• Descriptor: Outer membrane protein A (1 entity in total)
• Functional Keywords: membrane protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 17200.13

Authors

Johansson, M.U.,Alioth, S.,Hu, K.,Walser, R.,Koebnik, R.,Pervushin, K. (deposition date: 2006-11-20, release date: 2007-07-03, Last modification date: 2024-11-20)

Primary citation

Johansson, M.U.,Alioth, S.,Hu, K.,Walser, R.,Koebnik, R.,Pervushin, K.
A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance
Biochemistry, 46:1128-1140, 2007

PubMed Abstract: 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.

PubMed: 17260943
DOI: 10.1021/bi061265e

Experimental method

SOLUTION NMR