|PROSITE documentation PDOC51652 [for PROSITE entry PS51653]|
Nidoviruses (Coronaviridae, Arteriviridae, and Roniviridae) feature the most complex genetic organization among plus-strand RNA viruses [E1,E2,E3]. Their replicase genes encode an exceptionally large number of nonstructural protein domains which mediate the key functions required for genomic RNA synthesis (replication) and subgenomic RNA (sgRNA) synthesis (transcription). They encode a nonstructural protein, called nsp10 in arteriviruses (AV) and nsp13 in coronaviruses (CV), that is comprised of a C-terminal nucleoside triphosphate-binding/helicase (Hel) motif and an N-terminal cysteine-rich zinc-binding domain (ZBD). The ZBD is critically involved in nidovirus replication and transcription by modulating the enzymatic activities of the helicase domain and other, yet unknown, mechanisms [1,2,3].
The ZBD is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. It consists of a RING-like module and treble-cleft zinc finger, together coordinating three Zn atoms (see <PDB:4N0O>). The N-terminal RING-like module has a notable binuclear structure with a cross-brace topology involving 6 Cys and 2 His residues that coordinate two zinc ions. The C-terminal zinc finger of ZBD adopts a treble-cleft fold distinct from that of the RING module. It coordinates one Zn ion with a C[H/C]C[C/H] pattern .
The profiles we developed cover the entire AV and CV ZBD domains.Last update:
April 2016 / Text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||van Dinten L.C. van Tol H. Gorbalenya A.E. Snijder E.J.|
|Title||The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis.|
|Source||J. Virol. 74:5213-5223(2000).|
|2||Authors||Seybert A. Posthuma C.C. van Dinten L.C. Snijder E.J. Gorbalenya A.E. Ziebuhr J.|
|Title||A complex zinc finger controls the enzymatic activities of nidovirus helicases.|
|Source||J. Virol. 79:696-704(2005).|
|3||Authors||Deng Z. Lehmann K.C. Li X. Feng C. Wang G. Zhang Q. Qi X. Yu L. Zhang X. Feng W. Wu W. Gong P. Tao Y. Posthuma C.C. Snijder E.J. Gorbalenya A.E. Chen Z.|
|Title||Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase.|
|Source||Nucleic Acids Res. 42:3464-3477(2014).|