From Proteopedia
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| - | [[Image:2rlz.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2rlz| PDB=2rlz | SCENE= }} | | {{STRUCTURE_2rlz| PDB=2rlz | SCENE= }} |
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| - | '''Solid-State MAS NMR structure of the dimer Crh'''
| + | ===Solid-State MAS NMR structure of the dimer Crh=== |
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| - | ==Overview==
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| - | In a wide variety of proteins, insolubility presents a challenge to structural biology, as X-ray crystallography and liquid-state NMR are unsuitable. Indeed, no general approach is available as of today for studying the three-dimensional structures of membrane proteins and protein fibrils. We here demonstrate, at the example of the microcrystalline model protein Crh, how high-resolution 3D structures can be derived from magic-angle spinning solid-state NMR distance restraints for fully labeled protein samples. First, we show that proton-mediated rare-spin correlation spectra, as well as carbon-13 spin diffusion experiments, provide enough short, medium, and long-range structural restraints to obtain high-resolution structures of this 2 x 10.4 kDa dimeric protein. Nevertheless, the large number of 13C/15N spins present in this protein, combined with solid-state NMR line widths of about 0.5-1 ppm, induces substantial ambiguities in resonance assignments, preventing 3D structure determination by using distance restraints uniquely assigned on the basis of their chemical shifts. In the second part, we thus demonstrate that an automated iterative assignment algorithm implemented in a dedicated solid-state NMR version of the program ARIA permits to resolve the majority of ambiguities and to calculate a de novo 3D structure from highly ambiguous solid-state NMR data, using a unique fully labeled protein sample. We present, using distance restraints obtained through the iterative assignment process, as well as dihedral angle restraints predicted from chemical shifts, the 3D structure of the fully labeled Crh dimer refined at a root-mean-square deviation of 1.33 A.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18284240}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18284240 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18284240}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2RLZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLZ OCA]. | + | 2RLZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLZ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Solid-state nmr]] | | [[Category: Solid-state nmr]] |
| | [[Category: Transport protein]] | | [[Category: Transport protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:04:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:08:09 2008'' |
Revision as of 20:08, 27 July 2008
Template:STRUCTURE 2rlz
Solid-State MAS NMR structure of the dimer Crh
Template:ABSTRACT PUBMED 18284240
About this Structure
2RLZ is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.
Reference
3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints., Loquet A, Bardiaux B, Gardiennet C, Blanchet C, Baldus M, Nilges M, Malliavin T, Bockmann A, J Am Chem Soc. 2008 Mar 19;130(11):3579-89. Epub 2008 Feb 20. PMID:18284240
Page seeded by OCA on Sun Jul 27 23:08:09 2008
