1a7d

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Revision as of 11:32, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1a7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a7d, resolution 1.8Å" /> '''CHLOROMET MYOHEMERYTH...)
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File:1a7d.gif


1a7d, resolution 1.8Å

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CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

OverviewOverview

Myohemerythrin (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.

About this StructureAbout this Structure

1A7D is a Single protein structure of sequence from Themiste zostericola with CL and CFO as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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