1DWR

MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH CO

1DWR の概要

• エントリーDOI: 10.2210/pdb1dwr/pdb
• 関連するPDBエントリー: 1AZI 1BJE 1DWS 1DWT 1HRM 1HSY 1RSE 1WLA 1XCH 1YMA 1YMB 1YMC
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (5 entities in total)
• 機能のキーワード: oxygen transport, respiratory protein
• 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: 17820.14

構造登録者

Chu, K.,Vojtechovsky, J.,McMahon, B.H.,Sweet, R.M.,Berendzen, J.,Schlichting, I. (登録日: 1999-12-11, 公開日: 2000-03-03, 最終更新日: 2023-12-06)

主引用文献

Chu, K.,Vojtechovsky, J.,Mcmahon, B.H.,Sweet, R.M.,Berendzen, J.,Schlichting, I.
Crystal Structure of a New Ligand Binding Intermediate in Wildtype Carbonmonoxy Myoglobin
Nature, 403:921-, 2000

PubMed Abstract: Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations, random mutagenesis and flash photolysis studies indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 A resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis.

PubMed: 10706294
DOI: 10.1038/35002641

実験手法

X-RAY DIFFRACTION (1.45 Å)