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<StructureSection load='1myt' size='340' side='right'caption='[[1myt]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='1myt' size='340' side='right'caption='[[1myt]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1myt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neothunnus_macropterus Neothunnus macropterus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MYT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1myt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thunnus_albacares Thunnus albacares]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myt OCA], [http://pdbe.org/1myt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1myt RCSB], [http://www.ebi.ac.uk/pdbsum/1myt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1myt ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myt OCA], [https://pdbe.org/1myt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myt RCSB], [https://www.ebi.ac.uk/pdbsum/1myt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYG_THUAL MYG_THUAL]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.  
[https://www.uniprot.org/uniprot/MYG_THUAL MYG_THUAL] 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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</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=1myt ConSurf].
</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=1myt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares) has been determined by molecular replacement methods and refined to a conventional R factor of 0.177 for all observed reflections in the range of 6.0-1.70 A resolution. Like other myoglobins for which a high-resolution structure is available, the polypeptide chain is organized into several helices that cooperate to form a hydrophobic pocket into which the heme prosthetic group is non-covalently bound; however, the D helix observed in other myoglobins is absent in myoglobin from yellowfin tuna and has been replaced with a random coil. As well, the A helix has a pronounced kink due to the presence of Pro16. The differences in structure between this and sperm whale myoglobin can be correlated with their reported dioxygen affinity and dissociation. The structure is in agreement with reported fluorescence data which show an increased Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin.
1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix.,Birnbaum GI, Evans SV, Przybylska M, Rose DR Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):283-9. PMID:15299440<ref>PMID:15299440</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1myt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Neothunnus macropterus]]
[[Category: Thunnus albacares]]
[[Category: Birnbaum, G I]]
[[Category: Birnbaum GI]]
[[Category: Evans, S V]]
[[Category: Evans SV]]
[[Category: Przybylska, M]]
[[Category: Przybylska M]]
[[Category: Rose, D R]]
[[Category: Rose DR]]
[[Category: Oxygen transport]]

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