1v81

File:1v81.gif

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Solution structures of ubiquitin at 30 bar and 3 kbar

OverviewOverview

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 StructureAbout this Structure

1V81 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

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

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