2mnh | pdb_00002mnh

Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings

spinqualitylabelsall models 2mnh, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mnh is a 1 chain structure with sequence from Escherichia coli str. k-12 substr. mc4100. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: B0814, BN896_0667, JW0799, ompX, YBIG (Escherichia coli str. K-12 substr. MC4100) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be obtained by measuring residual dipolar couplings (RDCs) with the outer membrane protein OmpX embedded in nanodiscs using Pf1 phage as an alignment medium. The presented collection of membrane protein RDCs in nanodiscs represents an important step toward more comprehensive structural and dynamical NMR-based investigations of membrane proteins in a natural bilayer environment. Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.,Bibow S, Carneiro MG, Sabo TM, Schwiegk C, Becker S, Riek R, Lee D Protein Sci. 2014 Jul;23(7):851-6. doi: 10.1002/pro.2482. Epub 2014 May 6. PMID:24752984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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