2HRV

2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2

Summary for 2HRV

• Entry DOI: 10.2210/pdb2hrv/pdb
• Descriptor: 2A CYSTEINE PROTEINASE, ZINC ION (3 entities in total)
• Functional Keywords: hydrolase (cysteine proteinase), hydrolase
• Biological source: Human rhinovirus 2
• Cellular location: 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
• Total number of polymer chains: 2
• Total formula weight: 32583.15

Authors

Petersen, J.F.W.,Cherney, M.M.,Liebig, H.-D.,Skern, T.,Kuechler, E.,James, M.N.G. (deposition date: 1999-04-29, release date: 2000-05-03, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.95 Å)