1HZL

SOLUTION STRUCTURES OF C-1027 APOPROTEIN AND ITS COMPLEX WITH THE AROMATIZED CHROMOPHORE

1HZL の概要

• エントリーDOI: 10.2210/pdb1hzl/pdb
• 関連するPDBエントリー: 1HZK
• NMR情報: BMRB: 4947
• 分子名称: C-1027 APOPROTEIN, C-1027 AROMATIZED CHROMOPHORE (2 entities in total)
• 機能のキーワード: chromoprotein, c-1027, apoprotein, aromatized chromophore, antibiotic
• 由来する生物種: Streptomyces globisporus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11351.62

構造登録者

Tanaka, T.,Fukuda-Ishisaka, S.,Hirama, M.,Otani, T. (登録日: 2001-01-25, 公開日: 2001-05-23, 最終更新日: 2024-10-30)

主引用文献

Tanaka, T.,Fukuda-Ishisaka, S.,Hirama, M.,Otani, T.
Solution structures of C-1027 apoprotein and its complex with the aromatized chromophore.
J.Mol.Biol., 309:267-283, 2001

PubMed Abstract: C-1027 is one of the most potent antitumor antibiotic chromoproteins, and is a 1:1 complex of an enediyne chromophore having DNA-cleaving ability and a carrier apoprotein. The three-dimensional solution structures of the 110 residue (10.5 kDa) C-1027 apoprotein and its complex with the aromatized chromophore have been determined separately by homonuclear two-dimensional nuclear magnetic resonance methods. The apoprotein is mainly composed of three antiparallel beta-sheets: four-stranded beta-sheet (43-45, 52-54; 30-38; 92-94; 104-106), three-stranded beta-sheet (4-6; 17-22; 61-66), and two-stranded beta-sheet (70-72; 83-85). The overall structure of the apoprotein is very similar to those of other chromoprotein apoproteins, such as neocarzinostatin and kedarcidin. A hydrophobic pocket with approximate dimensions of 14 A x 12 A x 8 A is formed by the four-stranded beta-sheet and the three loops (39-42; 75-79; 97-100). The holoprotein (complex form with the aromatized chromophore) structure reveals that the aromatized chromophore is bound to the hydrophobic pocket found in the apoprotein. The benzodihydropentalene core of the chromophore is located in the center of the pocket and other substituents (beta-tyrosine, benzoxazine, and aminosugar moieties) are arranged around the core. Major binding interactions between the apoprotein and the chromophore are likely the hydrophobic contacts between the core of the chromophore and the hydrophobic side-chains of the pocket-forming residues, which is supplemented by salt bridges and/or hydrogen bonds. Based on the holoprotein structure, we propose possible mechanisms for the stabilization and the release of chromophore by the apoprotein.

PubMed: 11491295
DOI: 10.1006/jmbi.2001.4621

実験手法

SOLUTION NMR