2j53
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SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.
OverviewOverview
The solution structure of the GB1 domain of protein G at a pressure of 2, kbar is presented. The structure was calculated as a change from an, energy-minimised low-pressure structure using (1)H chemical shifts. Two, separate changes can be characterised: a compression/distortion, which is, linear with pressure; and a stabilisation of an alternative folded state., On application of pressure, linear chemical shift changes reveal that the, backbone structure changes by about 0.2 A root mean square, and is, compressed by about 1% overall. The alpha-helix compresses, particularly, at the C-terminal end, and moves toward the beta-sheet, while the, beta-sheet is twisted, with the corners closest to the alpha-helix curling, up towards it. The largest changes in structure are along the second, beta-strand, which becomes more twisted. This strand is where the protein, binds to IgG. Curved chemical shift changes with pressure indicate that, high pressure also populates an alternative structure with a distortion, towards the C-terminal end of the helix, which is likely to be caused by, insertion of a water molecule. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
About this StructureAbout this Structure
2J53 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
ReferenceReference
Pressure-induced changes in the solution structure of the GB1 domain of protein G., Wilton DJ, Tunnicliffe RB, Kamatari YO, Akasaka K, Williamson MP, Proteins. 2007 Dec 12;. PMID:18076052
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