1DUK

WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN

1DUK の概要

• エントリーDOI: 10.2210/pdb1duk/pdb
• 関連するPDBエントリー: 1DTM 1IRC
• 分子名称: WILD-TYPE RECOMBINANT SPERM WHALE METAQUOMYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: oxygen-storage protein, myoglobin, heme protein, oxygen storage-transport complex, oxygen storage/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: 17851.44

構造登録者

Barrick, D.,Dahlquist, F.W. (登録日: 2000-01-17, 公開日: 2000-02-07, 最終更新日: 2024-02-07)

主引用文献

Barrick, D.,Dahlquist, F.W.
Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion.
Proteins, 39:278-290, 2000

PubMed Abstract: The structural role of a side-chain to side-chain protein hydrogen bond is examined using trans-substitution of the proximal histidine of myoglobin with methylimidazoles (Barrick, Biochemistry 1994;33:6546-6554). Modification of the chemical structure of exogenous ligands allows this hydrogen bond to be disrupted. Comparison of the crystal structures of H93G myoglobin complexed 4-methylimidazole (4meimd; methylation at carbon 4) and 1-methylimidazole (1meimd; methylation at the adjacent nitrogen, preventing hydrogen bonding between the imidazole ligand and the protein) shows that the polypeptide, heme, and methylimidazole orientations are the same within error. For 4meimd there appear to be major and minor conformations corresponding to different tautomeric states of the ligand. Conformational heterogeneity is also seen in the hyperfine-shifted region of the NMR spectrum of 4meimd complexed with high-spin H93G deoxyMb. The major conformation of the 4meimd ligand and the 1meimd ligand, as seen in the respective crystal structures, are quite similar except that the proximal ligand NH-to-Ser92-OH hydrogen bond is eliminated in the 1meimd complex, and instead the proximal ligand CH is adjacent to the Ser92-OH. Thus, this system provides a means to eliminate the Mb proximal hydrogen bond in a chemically and structurally conservative way.

PubMed: 10813811
DOI: 10.1002/(SICI)1097-0134(20000601)39:4<278::AID-PROT20>3.0.CO;2-T

実験手法

X-RAY DIFFRACTION (2.13 Å)