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2j52

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[[Image:2j52.jpg|left|200px]]
 
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{{Structure
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==Solution Structure of GB1 domain Protein G and low and high pressure.==
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|PDB= 2j52 |SIZE=350|CAPTION= <scene name='initialview01'>2j52</scene>
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<StructureSection load='2j52' size='340' side='right'caption='[[2j52]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2j52]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2J52 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j52 OCA], [https://pdbe.org/2j52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j52 RCSB], [https://www.ebi.ac.uk/pdbsum/2j52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j52 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[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]]
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== Function ==
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2j52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j52 RCSB]</span>
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[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j5/2j52_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2j52 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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2J52 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=2J52 OCA].
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==Reference==
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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]
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[[Category: Single protein]]
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[[Category: Streptococcus sp.]]
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[[Category: Akasaka, K.]]
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[[Category: Kamatari, Y O.]]
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[[Category: Tunnicliffe, R B.]]
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[[Category: Williamson, M P.]]
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[[Category: Wilton, D J.]]
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[[Category: cell wall]]
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[[Category: igg-binding protein]]
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[[Category: immunoglobulin]]
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[[Category: peptidoglycan-anchor]]
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[[Category: pressure]]
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[[Category: protein g]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:08 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j52" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus sp]]
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[[Category: Akasaka K]]
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[[Category: Kamatari YO]]
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[[Category: Tunnicliffe RB]]
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[[Category: Williamson MP]]
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[[Category: Wilton DJ]]

Current revision

Solution Structure of GB1 domain Protein G and low and high pressure.

PDB ID 2j52

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