2HRV

2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2

2HRV の概要

• エントリーDOI: 10.2210/pdb2hrv/pdb
• 分子名称: 2A CYSTEINE PROTEINASE, ZINC ION (3 entities in total)
• 機能のキーワード: hydrolase (cysteine proteinase), hydrolase
• 由来する生物種: Human rhinovirus 2
• 細胞内の位置: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P04936
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32583.15

構造登録者

Petersen, J.F.W.,Cherney, M.M.,Liebig, H.-D.,Skern, T.,Kuechler, E.,James, M.N.G. (登録日: 1999-04-29, 公開日: 2000-05-03, 最終更新日: 2023-12-27)

主引用文献

Petersen, J.F.,Cherney, M.M.,Liebig, H.D.,Skern, T.,Kuechler, E.,James, M.N.
The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis.
EMBO J., 18:5463-5475, 1999

PubMed Abstract: The crystal structure of the 2A proteinase from human rhinovirus serotype 2 (HRV2-2A(pro)) has been solved to 1.95 A resolution. The structure has an unusual, although chymotrypsin-related, fold comprising a unique four-stranded beta sheet as the N-terminal domain and a six-stranded beta barrel as the C-terminal domain. A tightly bound zinc ion, essential for the stability of HRV2-2A(pro), is tetrahedrally coordinated by three cysteine sulfurs and one histidine nitrogen. The active site consists of a catalytic triad formed by His18, Asp35 and Cys106. Asp35 is additionally involved in an extensive hydrogen-bonding network. Modelling studies reveal a substrate-induced fit that explains the specificity of the subsites S4, S2, S1 and S1'. The structure of HRV2-2A(pro) suggests the mechanism of the cis cleavage and its release from the polyprotein.

PubMed: 10523291
DOI: 10.1093/emboj/18.20.5463

実験手法

X-RAY DIFFRACTION (1.95 Å)