2j53
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:2j53.jpg|left|200px]] | + | [[Image:2j53.jpg|left|200px]] |
- | + | ||
- | '''SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.''' | + | {{Structure |
+ | |PDB= 2j53 |SIZE=350|CAPTION= <scene name='initialview01'>2j53</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 2J53 is a [ | + | 2J53 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J53 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18076052 18076052] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
Line 25: | Line 34: | ||
[[Category: protein g]] | [[Category: protein g]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:37:20 2008'' |
Revision as of 15:37, 20 March 2008
| |||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Mar 20 17:37:20 2008