1NPG

MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITROSOETHANE

1NPG の概要

• エントリーDOI: 10.2210/pdb1npg/pdb
• 関連するPDBエントリー: 1NPF
• 分子名称: Myoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: heme, oxygen storage, nitric oxide, nitrosoethane, myoglobin, nitrosoalkane, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17851.19

構造登録者

Copeland, D.M.,West, A.H.,Richter-Addo, G.B. (登録日: 2003-01-17, 公開日: 2003-11-11, 最終更新日: 2023-08-16)

主引用文献

Copeland, D.M.,West, A.H.,Richter-Addo, G.B.
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane.
Proteins, 53:182-192, 2003

PubMed Abstract: The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO-containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of horse heart (hh) MbNO from nitrosylation of aqua-metMb crystals, and we have determined the crystal structure of hh MbNO at a resolution of 1.9 A. The Fe-N-O angle of 147 degrees in hh MbNO is larger than the corresponding 112 degrees angle previously determined from the crystal structure of sperm whale MbNO (Brucker et al., Proteins 1998;30:352-356) but is similar to the 150 degrees angle determined from a MS XAFS study of a frozen solution of hh MbNO (Rich et al., J Am Chem Soc 1998;120:10827-10836). The Fe-N(O) bond length of 2.0 A (this work) is longer than the 1.75 A distance determined from the XAFS study and suggests distal pocket influences on FeNO geometry. The nitrosyl N atom is located 3.0 A from the imidazole N(epsilon) atom of the distal His64 residue, suggesting electrostatic stabilization of the FeNO moiety by His64. The crystal structure of the nitrosoethane adduct of ferrous hh Mb was determined at a resolution of 1.7 A. The nitroso O atom of the EtNO ligand is located 2.7 A from the imidazole N(epsilon) atom of His64, suggesting a hydrogen bond interaction between these groups. To the best of our knowledge, the crystal structure of hh Mb(EtNO) is the first such determination of a nitrosoalkane adduct of a heme protein.

PubMed: 14517970
DOI: 10.1002/prot.10495

実験手法

X-RAY DIFFRACTION (1.7 Å)