2j53
From Proteopedia
(New page: 200px<br /><applet load="2j53" size="350" color="white" frame="true" align="right" spinBox="true" caption="2j53" /> '''SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G A...) |
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==Overview== | ==Overview== | ||
| - | The solution structure of the GB1 domain of protein G at a pressure of 2 | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
[[Category: Akasaka, K.]] | [[Category: Akasaka, K.]] | ||
| - | [[Category: Kamatari, Y | + | [[Category: Kamatari, Y O.]] |
| - | [[Category: Tunnicliffe, R | + | [[Category: Tunnicliffe, R B.]] |
| - | [[Category: Williamson, M | + | [[Category: Williamson, M P.]] |
| - | [[Category: Wilton, D | + | [[Category: Wilton, D J.]] |
[[Category: cell wall]] | [[Category: cell wall]] | ||
[[Category: igg-binding protein]] | [[Category: igg-binding protein]] | ||
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[[Category: protein g]] | [[Category: protein g]] | ||
| - | ''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 17:59:16 2008'' |
Revision as of 15:59, 21 February 2008
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SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.
Overview
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 Structure
2J53 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:59:16 2008
