1a7d: 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=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [http://www.ebi.ac.uk/pdbsum/1a7d 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=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [http://www.ebi.ac.uk/pdbsum/1a7d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/HEMTM_THEZO HEMTM_THEZO]] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:31, 25 December 2014
CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLACHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA
Structural highlights
Function[HEMTM_THEZO] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMyohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor muscles of marine "peanut" worms. The X-ray crystal structures of two recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A. Surprisingly, the met wild-type structure (R = 17.8%) was found to contain chloride bound to Fe2, while coordinated hydroxide was found in the met L103N structure (R = 18.3%). An internal water molecule was also found distal to the Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent with the kinetic and spectroscopic results reported for the L103N mutant Mhr [Raner, G. M., Martins, L. J., & Ellis, W. R., Jr. (1997) Biochemistry 36, 7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type Mhr) in gating ligand binding are also discussed. Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.,Martins LJ, Hill CP, Ellis WR Jr Biochemistry. 1997 Jun 10;36(23):7044-9. PMID:9188702[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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