2nrl: Difference between revisions

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-{{Seed}}
-[[Image:2nrl.png|left|200px]]
-<!--
+==Blackfin tuna myoglobin==
-The line below this paragraph, containing "STRUCTURE_2nrl", creates the "Structure Box" on the page.
+<StructureSection load='2nrl' size='340' side='right'caption='[[2nrl]], [[Resolution|resolution]] 0.91&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2nrl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thunnus_atlanticus Thunnus atlanticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NRL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.91&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-{{STRUCTURE_2nrl|  PDB=2nrl  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nrl OCA], [https://pdbe.org/2nrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nrl RCSB], [https://www.ebi.ac.uk/pdbsum/2nrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nrl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MYG_THUOR MYG_THUOR] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+== 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/nr/2nrl_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2nrl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+S-nitrosylation is a post-translational protein modification that can alter the function of a variety of proteins. Despite the growing wealth of information that this modification may have important functional consequences, little is known about the structure of the moiety or its effect on protein tertiary structure. Here we report high-resolution x-ray crystal structures of S-nitrosylated and unmodified blackfin tuna myoglobin, which demonstrate that in vitro S-nitrosylation of this protein at the surface-exposed Cys-10 directly causes a reversible conformational change by "wedging" apart a helix and loop. Furthermore, we have demonstrated in solution and in a single crystal that reduction of the S-nitrosylated myoglobin with dithionite results in NO cleavage from the sulfur of Cys-10 and rebinding to the reduced heme iron, showing the reversibility of both the modification and the conformational changes. Finally, we report the 0.95-A structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.
-===Blackfin tuna myoglobin===
+S-nitrosylation-induced conformational change in blackfin tuna myoglobin.,Schreiter ER, Rodriguez MM, Weichsel A, Montfort WR, Bonaventura J J Biol Chem. 2007 Jul 6;282(27):19773-80. Epub 2007 May 8. PMID:17488722<ref>PMID:17488722</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2nrl" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17488722}}, adds the Publication Abstract to the page
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17488722 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17488722}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRL OCA].
+[[Category: Thunnus atlanticus]]
+[[Category: Bonaventura J]]
-==Reference==
+[[Category: Montfort WR]]
-S-nitrosylation-induced conformational change in blackfin tuna myoglobin., Schreiter ER, Rodriguez MM, Weichsel A, Montfort WR, Bonaventura J, J Biol Chem. 2007 Jul 6;282(27):19773-80. Epub 2007 May 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17488722 17488722]
+[[Category: Rodr guez MM]]
-[[Category: Bonaventura, J.]]
+[[Category: Schreiter ER]]
-[[Category: Montfort, W R.]]
+[[Category: Weichsel A]]
-[[Category: Schreiter, E R.]]
-[[Category: Weichsel, A.]]
-[[Category: Guez, M M.Rodr.]]
-[[Category: Globin]]
-[[Category: Myoglobin]]
-[[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:22:36 2008''