1myt: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1myt]] is a 1 chain structure with sequence from [http://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 [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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MYT FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>< | </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> | ||
<tr><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://www.rcsb.org/pdb/explore.do?structureId=1myt RCSB], [http://www.ebi.ac.uk/pdbsum/1myt PDBsum]</span></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://www.rcsb.org/pdb/explore.do?structureId=1myt RCSB], [http://www.ebi.ac.uk/pdbsum/1myt PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thunnus albacares]] | [[Category: Thunnus albacares]] | ||
[[Category: Birnbaum, G I | [[Category: Birnbaum, G I]] | ||
[[Category: Evans, S V | [[Category: Evans, S V]] | ||
[[Category: Przybylska, M | [[Category: Przybylska, M]] | ||
[[Category: Rose, D R | [[Category: Rose, D R]] | ||
[[Category: Oxygen transport]] | [[Category: Oxygen transport]] | ||
Revision as of 03:12, 25 December 2014
CRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIXCRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIX
Structural highlights
Function[MYG_THUAL] 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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||