2j52: Difference between revisions
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[[Image: | ==SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.== | ||
<StructureSection load='2j52' size='340' side='right' caption='[[2j52]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2j52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J52 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1em7|1em7]], [[1gb1|1gb1]], [[1igc|1igc]], [[1igd|1igd]], [[1le3|1le3]], [[1mpe|1mpe]], [[1mvk|1mvk]], [[1pga|1pga]], [[1pgb|1pgb]], [[1pgx|1pgx]], [[1pn5|1pn5]], [[1q10|1q10]], [[2gb1|2gb1]], [[2igd|2igd]], [[2igh|2igh]], [[2j53|2j53]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j52 RCSB], [http://www.ebi.ac.uk/pdbsum/2j52 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j5/2j52_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:18076052</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
[[Category: Akasaka, K.]] | [[Category: Akasaka, K.]] | ||
Revision as of 10:47, 30 September 2014
SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.
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