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5d5r

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Horse-heart myoglobin - deoxy state

Structural highlights

5d5r 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.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d5r"

Categories: Equus caballus | Large Structures | Barends T | Schlichting I

@@ Line 3: / Line 3: @@
 <StructureSection load='5d5r' size='340' side='right'caption='[[5d5r]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d5r]] 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=5D5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5R FirstGlance]. <br>
+<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]] 1.6&#8491;</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=5d5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5r OCA], [http://pdbe.org/5d5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5r RCSB], [http://www.ebi.ac.uk/pdbsum/5d5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5r ProSAT]</span></td></tr>
+<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>
 == 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.
+[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 ==
@@ Line 27: / Line 28: @@
 [[Category: Equus caballus]]
 [[Category: Large Structures]]
-[[Category: Barends, T]]
+[[Category: Barends T]]
-[[Category: Schlichting, I]]
+[[Category: Schlichting I]]
-[[Category: Heme protein]]
-[[Category: Myoglobin]]
-[[Category: Oxygen storage]]

5d5r

From Proteopedia

Current revision

Horse-heart myoglobin - deoxy state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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