1orm

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(New page: 200px<br /><applet load="1orm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orm" /> '''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX ...)
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Revision as of 21:00, 20 November 2007

Image:1orm.jpg

1orm

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NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES

Overview

The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX, from Escherichia coli was reconstituted with dihexanoyl, phosphatidylcholine (DHPC) in mixed micelles of molecular mass of about 60, kDa. Transverse relaxation-optimized spectroscopy (TROSY)-type triple, resonance NMR experiments and TROSY-type nuclear Overhauser enhancement, spectra were recorded in 2 mM aqueous solutions of these mixed micelles at, pH 6.8 and 30 degrees C. Complete sequence-specific NMR assignments for, the polypeptide backbone thus have been obtained. The (13)C chemical, shifts and the nuclear Overhauser effect data then resulted in the, identification of the regular secondary structure elements of OmpX/DHPC in, solution and in the collection of an input of conformational constraints, for the computation of the global fold of the protein. The same type of, polypeptide backbone fold is observed in the presently determined solution, structure and the previously reported crystal structure of OmpX determined, in the presence of the detergent n-octyltetraoxyethylene. Further, structure refinement will have to rely on the additional resonance, assignment of partially or fully protonated amino acid side chains, but, the present data already demonstrate that relaxation-optimized NMR, techniques open novel avenues for studies of structure and function of, integral membrane proteins.

About this Structure

1ORM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles., Fernandez C, Adeishvili K, Wuthrich K, Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2358-63. Epub 2001 Feb 20. PMID:11226244

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