2h3o: Difference between revisions
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[[Image:2h3o.gif|left|200px]] | [[Image:2h3o.gif|left|200px]] | ||
'''Structure of MERFT, a membrane protein with two trans-membrane helices''' | {{Structure | ||
|PDB= 2h3o |SIZE=350|CAPTION= <scene name='initialview01'>2h3o</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= merF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=582 Morganella morganii]) | |||
}} | |||
'''Structure of MERFT, a membrane protein with two trans-membrane helices''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2H3O is a [ | 2H3O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Morganella_morganii Morganella morganii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H3O OCA]. | ||
==Reference== | ==Reference== | ||
Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy., De Angelis AA, Howell SC, Nevzorov AA, Opella SJ, J Am Chem Soc. 2006 Sep 20;128(37):12256-67. PMID:[http:// | Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy., De Angelis AA, Howell SC, Nevzorov AA, Opella SJ, J Am Chem Soc. 2006 Sep 20;128(37):12256-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16967977 16967977] | ||
[[Category: Morganella morganii]] | [[Category: Morganella morganii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
''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 17:12:12 2008'' |
Revision as of 18:12, 20 March 2008
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Gene: | merF (Morganella morganii) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of MERFT, a membrane protein with two trans-membrane helices
OverviewOverview
The structure of the membrane protein MerFt was determined in magnetically aligned phospholipid bicelles by solid-state NMR spectroscopy. With two trans-membrane helices and a 10-residue inter-helical loop, this truncated construct of the mercury transport membrane protein MerF has sufficient structural complexity to demonstrate the feasibility of determining the structures of polytopic membrane proteins in their native phospholipid bilayer environment under physiological conditions. PISEMA, SAMMY, and other double-resonance experiments were applied to uniformly and selectively (15)N-labeled samples to resolve and assign the backbone amide resonances and to measure the associated (15)N chemical shift and (1)H-(15)N heteronuclear dipolar coupling frequencies as orientation constraints for structure calculations. (1)H/(13)C/(15)N triple-resonance experiments were applied to selectively (13)C'- and (15)N-labeled samples to complete the resonance assignments, especially for residues in the nonhelical regions of the protein. A single resonance is observed for each labeled site in one- and two-dimensional spectra. Therefore, each residue has a unique conformation, and all protein molecules in the sample have the same three-dimensional structure and are oriented identically in planar phospholipid bilayers. Combined with the absence of significant intensity near the isotropic resonance frequency, this demonstrates that the entire protein, including the loop and terminal regions, has a well-defined, stable structure in phospholipid bilayers.
About this StructureAbout this Structure
2H3O is a Single protein structure of sequence from Morganella morganii. Full crystallographic information is available from OCA.
ReferenceReference
Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy., De Angelis AA, Howell SC, Nevzorov AA, Opella SJ, J Am Chem Soc. 2006 Sep 20;128(37):12256-67. PMID:16967977
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