3wft: Difference between revisions

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<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=3wft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wft OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wft RCSB], [http://www.ebi.ac.uk/pdbsum/3wft PDBsum]</span></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=3wft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wft OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wft RCSB], [http://www.ebi.ac.uk/pdbsum/3wft PDBsum]</span></td></tr>
</table>
</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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 03:26, 25 December 2014

Crystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrinCrystal structure of horse heart myoglobin reconstituted with cobalt(II) tetradehydrocorrin

Structural highlights

3wft 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, RCSB, PDBsum

Function

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

Publication Abstract from PubMed

A conjugate between apomyoglobin and cobalt tetradehydrocorrin was prepared to replicate the coordination behavior of cob(I)alamin in methionine synthase. X-ray crystallography reveals that the tetra-coordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket.

Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model.,Hayashi T, Morita Y, Mizohata E, Oohora K, Ohbayashi J, Inoue T, Hisaeda Y Chem Commun (Camb). 2014 Oct 25;50(83):12560-3. doi: 10.1039/c4cc05448b. PMID:25197974[1]

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

References

  1. Hayashi T, Morita Y, Mizohata E, Oohora K, Ohbayashi J, Inoue T, Hisaeda Y. Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model. Chem Commun (Camb). 2014 Oct 25;50(83):12560-3. doi: 10.1039/c4cc05448b. PMID:25197974 doi:http://dx.doi.org/10.1039/c4cc05448b

3wft, resolution 1.30Å

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