1JDO

SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)

1JDO の概要

• エントリーDOI: 10.2210/pdb1jdo/pdb
• 分子名称: MYOGLOBIN, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: globin, heme, oxygen storage, nitric oxide, oxygen transport
• 由来する生物種: Physeter catodon (sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18141.74

構造登録者

Brucker, E.A.,Phillips Jr., G.N. (登録日: 1998-02-10, 公開日: 1998-05-27, 最終更新日: 2024-05-22)

主引用文献

Brucker, E.A.,Olson, J.S.,Ikeda-Saito, M.,Phillips Jr., G.N.
Nitric oxide myoglobin: crystal structure and analysis of ligand geometry.
Proteins, 30:352-356, 1998

PubMed Abstract: The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold.

PubMed: 9533619
DOI: 10.1002/(SICI)1097-0134(19980301)30:4<352::AID-PROT2>3.3.CO;2-G

実験手法

X-RAY DIFFRACTION (1.9 Å)