1orm
From Proteopedia
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| - | [[Image:1orm.jpg|left|200px]] | + | [[Image:1orm.jpg|left|200px]] |
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| - | '''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES''' | + | {{Structure |
| + | |PDB= 1orm |SIZE=350|CAPTION= <scene name='initialview01'>1orm</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= OMPX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ORM is a [ | + | 1ORM is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11226244 11226244] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Fernandez, C.]] | [[Category: Fernandez, C.]] | ||
[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
| - | [[Category: | + | [[Category: detergent]] |
[[Category: dhpc]] | [[Category: dhpc]] | ||
| - | [[Category: | + | [[Category: lipid]] |
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | [[Category: | + | [[Category: micelle]] |
[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: ompx]] | [[Category: ompx]] | ||
[[Category: trosy]] | [[Category: trosy]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:39 2008'' |
Revision as of 11:14, 20 March 2008
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| Gene: | OMPX (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 13:14:39 2008
Categories: Escherichia coli | Single protein | Adeishvili, K. | Fernandez, C. | Wuthrich, K. | Detergent | Dhpc | Lipid | Membrane protein | Micelle | Nmr | Ompx | Trosy
