2j53: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2j53.jpg|left|200px]]<br /><applet load="2j53" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2j53" />
-'''SOLUTION STRUCTURE OF GB1 DOMAIN PROTEIN G AND LOW AND HIGH PRESSURE.'''<br />
-==Overview==
+==Solution Structure of GB1 domain Protein G and low and high pressure.==
-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.
+<StructureSection load='2j53' size='340' side='right'caption='[[2j53]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2j53]] 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=2J53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J53 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j53 OCA], [https://pdbe.org/2j53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j53 RCSB], [https://www.ebi.ac.uk/pdbsum/2j53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j53 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
+== 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/j5/2j53_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/main_output.php?pdb_ID=2j53 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.
-==About this Structure==
+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>
-J53 is a [http://en.wikipedia.org/wiki/Single_protein 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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076052 18076052]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 2j53" style="background-color:#fffaf0;"></div>
-[[Category: Streptococcus sp.]]
+== References ==
-[[Category: Akasaka, K.]]
+<references/>
-[[Category: Kamatari, Y.O.]]
+__TOC__
-[[Category: Tunnicliffe, R.B.]]
+</StructureSection>
-[[Category: Williamson, M.P.]]
+[[Category: Large Structures]]
-[[Category: Wilton, D.J.]]
+[[Category: Streptococcus sp]]
-[[Category: cell wall]]
+[[Category: Akasaka K]]
-[[Category: igg-binding protein]]
+[[Category: Kamatari YO]]
-[[Category: immunoglobulin]]
+[[Category: Tunnicliffe RB]]
-[[Category: peptidoglycan-anchor]]
+[[Category: Williamson MP]]
-[[Category: pressure]]
+[[Category: Wilton DJ]]
-[[Category: protein g]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:22:33 2008''