1orm
From Proteopedia
(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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'''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES'''<br /> | '''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX | + | 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== | ==About this Structure== | ||
| - | 1ORM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1ORM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trosy]] | [[Category: trosy]] | ||
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Revision as of 12:20, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 14:20:48 2008
Categories: Escherichia coli | Single protein | Adeishvili, K. | Fernandez, C. | Wuthrich, K. | Detergents | Dhpc | Lipids | Membrane protein | Micelles | Nmr | Ompx | Trosy
