1A7D

CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA

1A7D の概要

• エントリーDOI: 10.2210/pdb1a7d/pdb
• 分子名称: MYOHEMERYTHRIN, CHLORIDE ION, CHLORO DIIRON-OXO MOIETY, ... (4 entities in total)
• 機能のキーワード: nonheme iron oxygen carrier, oxygen transport
• 由来する生物種: Themiste zostericola
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14034.79

構造登録者

Martins, L.J.,Hill, C.P.,Ellis Junior, W.R. (登録日: 1998-03-12, 公開日: 1998-10-14, 最終更新日: 2024-02-07)

主引用文献

Martins, 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

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

実験手法

X-RAY DIFFRACTION (1.8 Å)