1v80
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Conformational fluctuation plays a key role in protein function, but we | + | 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== | ==About this Structure== | ||
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[[Category: Akasaka, K.]] | [[Category: Akasaka, K.]] | ||
[[Category: Kitahara, R.]] | [[Category: Kitahara, R.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: national project on protein structural and functional analyses]] | [[Category: national project on protein structural and functional analyses]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:25 2008'' |
Revision as of 13:32, 21 February 2008
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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 Thu Feb 21 15:32:25 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 analyses | Nppsfa | Pressure | Riken structural genomics/proteomics initiative | Rsgi | Signaling protein | Structural genomics
