Literature summary for 3.4.22.B79 extracted from

Russo, A.T.; White, M.A.; Watowich, S.J.
The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease (2006), Structure, 14, 1449-1458.

Search for more literature for 3.4.22.B79

Application

Application	Comment	Organism
medicine	the nsp2pro N-terminal domain is a novel cysteine protease fold. the C-terminal domain displays structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases. This structure will significantly aid drug discovery and development efforts to combat Venezuelan equine encephalitis alphavirus and related viruses	Venezuelan equine encephalitis virus

Cloned(Commentary)

Cloned (Comment)	Organism
DNA coding for nsP2pro (residues Met457-Cys794) amplified and cloned into vector pETBlue1 T7. Expression in Tuner DE3 (pLacI) Escherichia coli cells	Venezuelan equine encephalitis virus

Crystallization (Commentary)

Crystallization (Comment)	Organism
at 2.45 A resolution. Belongs to space group P212121. N-terminal domain (Asp468 to Asn603) contains the catalytic dyad formed by Cys477 and His546, organized in a protein fold. C-terminal domain (Arg604 to Ser793) contributes to substrate recognition and regulates the structure of the substrate binding cleft	Venezuelan equine encephalitis virus

Organism

Organism	UniProt	Comment	Textmining
Venezuelan equine encephalitis virus	P27282	-	-

Purification (Commentary)

Purification (Comment)	Organism
by gel filtration, more than 99% pure	Venezuelan equine encephalitis virus

Synonyms

Synonyms	Comment	Organism
nsP2 protease	-	Venezuelan equine encephalitis virus

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Release 2023.1 (January 2023)