5cn8: Difference between revisions

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m Protected "5cn8" [edit=sysop:move=sysop]
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'''Unreleased structure'''
==Ultrafast dynamics in myoglobin: 0.3 ps time delay==
<StructureSection load='5cn8' size='340' side='right' caption='[[5cn8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cn8]] 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=5CN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CN8 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>
<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=5cn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cn8 OCA], [http://pdbe.org/5cn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cn8 RCSB], [http://www.ebi.ac.uk/pdbsum/5cn8 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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.


The entry 5cn8 is ON HOLD
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>


Authors: Barends, T.R.M., Foucar, L., Ardevol, A., Nass, K.J., Aquila, A., Botha, S., Doak, R.B., Falahati, K., Hartmann, E., Hilpert, M., Heinz, M., Hoffmann, M.C., Koefinger, J., Koglin, J., Kovacsova, G., Liang, M., Milathianaki, D., Lemke, H.T., Reinstein, J., Roome, C.M., Shoeman, R.L., Williams, G.J., Burghardt, I., Hummer, G., Boutet, S., Schlichting, I.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description:  
<div class="pdbe-citations 5cn8" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Liang, M]]
<references/>
[[Category: Shoeman, R.L]]
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Aquila, A]]
[[Category: Ardevol, A]]
[[Category: Ardevol, A]]
[[Category: Barends, T R.M]]
[[Category: Botha, S]]
[[Category: Botha, S]]
[[Category: Barends, T.R.M]]
[[Category: Boutet, S]]
[[Category: Williams, G.J]]
[[Category: Reinstein, J]]
[[Category: Hoffmann, M.C]]
[[Category: Aquila, A]]
[[Category: Burghardt, I]]
[[Category: Burghardt, I]]
[[Category: Boutet, S]]
[[Category: Doak, R B]]
[[Category: Falahati, K]]
[[Category: Foucar, L]]
[[Category: Hartmann, E]]
[[Category: Heinz, M]]
[[Category: Hilpert, M]]
[[Category: Hilpert, M]]
[[Category: Lemke, H.T]]
[[Category: Hoffmann, M C]]
[[Category: Hummer, G]]
[[Category: Koefinger, J]]
[[Category: Koefinger, J]]
[[Category: Heinz, M]]
[[Category: Koglin, J]]
[[Category: Foucar, L]]
[[Category: Kovacsova, G]]
[[Category: Lemke, H T]]
[[Category: Liang, M]]
[[Category: Milathianaki, D]]
[[Category: Milathianaki, D]]
[[Category: Doak, R.B]]
[[Category: Nass, K J]]
[[Category: Reinstein, J]]
[[Category: Roome, C M]]
[[Category: Schlichting, I]]
[[Category: Schlichting, I]]
[[Category: Nass, K.J]]
[[Category: Shoeman, R L]]
[[Category: Koglin, J]]
[[Category: Williams, G J]]
[[Category: Falahati, K]]
[[Category: Carbon monoxide]]
[[Category: Roome, C.M]]
[[Category: Free-electron laser]]
[[Category: Kovacsova, G]]
[[Category: Oxygen storage]]
[[Category: Hummer, G]]
[[Category: Protein dynamic]]
[[Category: Hartmann, E]]
[[Category: Serial femtosecond crystallography]]
[[Category: Time-resolved crystallography]]

Revision as of 09:17, 30 September 2015

Ultrafast dynamics in myoglobin: 0.3 ps time delayUltrafast dynamics in myoglobin: 0.3 ps time delay

Structural highlights

5cn8 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ 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. Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation. Science. 2015 Sep 10. pii: aac5492. PMID:26359336 doi:http://dx.doi.org/10.1126/science.aac5492

5cn8, resolution 1.80Å

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