2hrv
From Proteopedia
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2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2
Overview
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.
About this Structure
2HRV is a Single protein structure of sequence from Human rhinovirus 2 with ZN as ligand. Active as Picornain 2A, with EC number 3.4.22.29 Full crystallographic information is available from OCA.
Reference
The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis., Petersen JF, Cherney MM, Liebig HD, Skern T, Kuechler E, James MN, EMBO J. 1999 Oct 15;18(20):5463-75. PMID:10523291
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