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1A7D

CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

Summary for 1A7D
Entry DOI10.2210/pdb1a7d/pdb
DescriptorMYOHEMERYTHRIN, CHLORIDE ION, CHLORO DIIRON-OXO MOIETY, ... (4 entities in total)
Functional Keywordsnonheme iron oxygen carrier, oxygen transport
Biological sourceThemiste zostericola
Total number of polymer chains1
Total formula weight14034.79
Authors
Martins, L.J.,Hill, C.P.,Ellis Junior, W.R. (deposition date: 1998-03-12, release date: 1998-10-14, Last modification date: 2024-02-07)
Primary citationMartins, L.J.,Hill, C.P.,Ellis Jr., W.R.
Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.
Biochemistry, 36:7044-7049, 1997
Cited by
PubMed Abstract: 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.
PubMed: 9188702
DOI: 10.1021/bi9630422
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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