5cn6: Difference between revisions
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==Ultrafast dynamics in myoglobin: 0.1 ps time delay== | ==Ultrafast dynamics in myoglobin: 0.1 ps time delay== | ||
<StructureSection load='5cn6' size='340' side='right' caption='[[5cn6]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5cn6' size='340' side='right'caption='[[5cn6]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CN6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5cn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CN6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5CN6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </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'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5cn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cn6 OCA], [http://pdbe.org/5cn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cn6 RCSB], [http://www.ebi.ac.uk/pdbsum/5cn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cn6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Myoglobin|Myoglobin]] | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | |||
[[Category: Aquila, A]] | [[Category: Aquila, A]] | ||
[[Category: Ardevol, A]] | [[Category: Ardevol, A]] | ||
Revision as of 10:06, 19 August 2020
Ultrafast dynamics in myoglobin: 0.1 ps time delayUltrafast dynamics in myoglobin: 0.1 ps time delay
Structural highlights
Function[MYG_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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Equus caballus
- Large Structures
- Aquila, A
- Ardevol, A
- Barends, T R.M
- Botha, S
- Boutet, S
- Burghardt, I
- Doak, R B
- Falahati, K
- Foucar, L
- Hartmann, E
- Heinz, M
- Hilpert, M
- Hoffmann, M C
- Hummer, G
- Koefinger, J
- Koglin, J
- Kovacsova, G
- Lemke, H T
- Liang, M
- Milathianaki, D
- Nass, K J
- Reinstein, J
- Roome, C M
- Schlichting, I
- Shoeman, R L
- Williams, G J
- Carbon monoxide
- Free-electron laser
- Oxygen storage
- Protein dynamic
- Serial femtosecond crystallography
- Time-resolved crystallography