5cmv: Difference between revisions
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New page: '''Unreleased structure''' The entry 5cmv is ON HOLD Authors: Barends, T.R.M., Foucar, L., Ardevol, A., Nass, Karol J., Aquila, A., Botha, S., Doak,R.B., Falahati, K., Hartmann, E., Hil... |
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The | ==Ultrafast dynamics in myoglobin: dark-state, CO-ligated structure== | ||
<StructureSection load='5cmv' size='340' side='right'caption='[[5cmv]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cmv]] 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=5CMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5cmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmv OCA], [https://pdbe.org/5cmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmv RCSB], [https://www.ebi.ac.uk/pdbsum/5cmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmv ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:26359336</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5cmv" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
[[Category: Botha | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Equus caballus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aquila A]] | ||
[[Category: | [[Category: Ardevol A]] | ||
[[Category: | [[Category: Barends TRM]] | ||
[[Category: | [[Category: Botha S]] | ||
[[Category: | [[Category: Boutet S]] | ||
[[Category: Koefinger | [[Category: Burghardt I]] | ||
[[Category: | [[Category: Doak RB]] | ||
[[Category: | [[Category: Falahati K]] | ||
[[Category: | [[Category: Foucar L]] | ||
[[Category: | [[Category: Hartmann E]] | ||
[[Category: | [[Category: Heinz M]] | ||
[[Category: | [[Category: Hilpert M]] | ||
[[Category: | [[Category: Hoffmann MC]] | ||
[[Category: | [[Category: Hummer G]] | ||
[[Category: | [[Category: Koefinger J]] | ||
[[Category: | [[Category: Koglin J]] | ||
[[Category: Kovacsova G]] | |||
[[Category: Lemke HT]] | |||
[[Category: Liang M]] | |||
[[Category: Milathianaki D]] | |||
[[Category: Nass KJ]] | |||
[[Category: Reinstein J]] | |||
[[Category: Roome CM]] | |||
[[Category: Schlichting I]] | |||
[[Category: Shoeman RL]] | |||
[[Category: Williams GJ]] | |||
Latest revision as of 14:21, 10 January 2024
Ultrafast dynamics in myoglobin: dark-state, CO-ligated structureUltrafast dynamics in myoglobin: dark-state, CO-ligated structure
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
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