1v80
From Proteopedia
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'''Solution structures of ubiquitin at 30 bar and 3 kbar''' | '''Solution structures of ubiquitin at 30 bar and 3 kbar''' | ||
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: National project on protein structural and functional analyse]] |
| - | [[Category: | + | [[Category: Nppsfa]] |
| - | [[Category: | + | [[Category: Pressure]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Signaling protein]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:11:49 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:11, 3 May 2008
Solution structures of ubiquitin at 30 bar and 3 kbar
Overview
Conformational fluctuation plays a key role in protein function, but we know little about the associated structural changes. Here we present a general method for elucidating, at the atomic level, a large-scale shape change of a protein molecule in solution undergoing conformational fluctuation. The method utilizes the intimate relationship between conformation and partial molar volume and determines three-dimensional structures of a protein at different pressures using variable pressure NMR technique, whereby NOE distance and torsion angle constraints are used to create average coordinates. Ubiquitin (pH 4.6 at 20 degrees C) was chosen as the first target, for which structures were determined at 30 bar and at 3 kbar, giving "NMR snapshots" of a fluctuating protein structure at atomic resolution. The result reveals that the helix swings in and out by >3 angstroms with a simultaneous reorientation of the C-terminal segment, providing an "open" conformer suitable for enzyme recognition. Spin relaxation analysis indicates that this fluctuation occurs in the ten microsecond time range with activation volumes -4.2(+/-3.2) and 18.5(+/-3.0) ml/mol for the "closed-to-open" and the "open-to-closed" transitions, respectively.
About this Structure
1V80 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar., Kitahara R, Yokoyama S, Akasaka K, J Mol Biol. 2005 Mar 25;347(2):277-85. PMID:15740740 Page seeded by OCA on Sat May 3 12:11:49 2008
Categories: Bos taurus | Single protein | Akasaka, K. | Kitahara, R. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | National project on protein structural and functional analyse | Nppsfa | Pressure | Riken structural genomics/proteomics initiative | Rsgi | Signaling protein | Structural genomic
