Literature summary for 2.7.7.48 extracted from

Shaik, M.M.; Bhattacharjee, N.; Feliks, M.; Ng, K.K.; Field, M.J.
Norovirus RNA-dependent RNA polymerase A computational study of metal-binding preferences (2017), Proteins, 85, 1435-1445 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
a complex of Norovirus RNA-dependent RNA polymerase bound to Mn2+ and an RNA primer-template duplex is investigated using X-ray crystallography and hybrid quantum chemical/molecular mechanical simulations. The complex crystallizes in a tetragonal crystal form. The nature of the primer/template duplex binding in the resulting structure indicates that the complex is a closed back-tracked state of the enzyme, in which the 3'-end of the primer occupies the position expected for the postincorporated nucleotide before translocation. Computationally, it is found that the complex can accept a range of divalent metal cations without marked distortions in the active site structure. The highest binding energy is for copper, followed closely by manganese and iron, and then by zinc, nickel, and cobalt	Norwalk virus

Crystallization (Comment)

Organism

a complex of Norovirus RNA-dependent RNA polymerase bound to Mn2+ and an RNA primer-template duplex is investigated using X-ray crystallography and hybrid quantum chemical/molecular mechanical simulations. The complex crystallizes in a tetragonal crystal form. The nature of the primer/template duplex binding in the resulting structure indicates that the complex is a closed back-tracked state of the enzyme, in which the 3'-end of the primer occupies the position expected for the postincorporated nucleotide before translocation. Computationally, it is found that the complex can accept a range of divalent metal cations without marked distortions in the active site structure. The highest binding energy is for copper, followed closely by manganese and iron, and then by zinc, nickel, and cobalt

Norwalk virus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	computational study of metal-binding preferences. When he calculated metal hydration energies are used, the proteination energies for the structures indicate that the binding preference for the metal is Cu2+ > Mn2+, Fe2+ > Zn2+ > Ni2+ > Co2+ > Mg2+, Ca2+	Norwalk virus

Organism

Organism	UniProt	Comment	Textmining
Norwalk virus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Norwalk virus

Synonyms

Synonyms	Comment	Organism
RDRP	-	Norwalk virus
RNA-dependent RNA polymerase	-	Norwalk virus

General Information

General Information	Comment	Organism
drug target	the enzyme is a key target for the development of antiviral agents against Norwalk virus gastroenteritis	Norwalk virus
physiological function	the enzyme is essential for replicating the genome of the virus	Norwalk virus