5d5r: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Horse-heart myoglobin - deoxy state== | ==Horse-heart myoglobin - deoxy state== | ||
<StructureSection load='5d5r' size='340' side='right' caption='[[5d5r]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5d5r' size='340' side='right'caption='[[5d5r]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d5r]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5d5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D5R 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]] 1.6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=5d5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5r OCA], [https://pdbe.org/5d5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d5r RCSB], [https://www.ebi.ac.uk/pdbsum/5d5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5d5r" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5d5r" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Barends T]] | ||
[[Category: | [[Category: Schlichting I]] | ||
Latest revision as of 14:24, 10 January 2024
Horse-heart myoglobin - deoxy stateHorse-heart myoglobin - deoxy state
Structural highlights
FunctionMYG_HORSE Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedThe hemoprotein myoglobin is a model system to study protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes taking place in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 fs with the C-, F- and H-helices moving away from the heme and the E- and A-helices moving toward it. These collective movements are predicted by quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, the calculations support predictions that an immediate collective response of the protein takes place upon ligand dissociation due to coupling of vibrational modes of the heme to global modes of the protein. Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation.,Barends TR, Foucar L, Ardevol A, Nass K, Aquila A, Botha S, Doak RB, Falahati K, Hartmann E, Hilpert M, Heinz M, Hoffmann MC, Kofinger J, Koglin JE, Kovacsova G, Liang M, Milathianaki D, Lemke H, Reinstein J, Roome CM, Shoeman RL, Williams GJ, Burghardt I, Hummer G, Boutet S, Schlichting I Science. 2015 Sep 10. pii: aac5492. PMID:26359336[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||