2nrl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.91Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thunnus atlanticus]] | [[Category: Thunnus atlanticus]] | ||
[[Category: Bonaventura | [[Category: Bonaventura J]] | ||
[[Category: Montfort | [[Category: Montfort WR]] | ||
[[Category: | [[Category: Rodr guez MM]] | ||
[[Category: Schreiter ER]] | |||
[[Category: Weichsel A]] | |||
[[Category: | |||
[[Category: | |||
Revision as of 13:19, 30 August 2023
Blackfin tuna myoglobinBlackfin tuna myoglobin
Structural highlights
FunctionMYG_THUOR Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedS-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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