Literature summary for 2.7.7.6 extracted from

Obayashi, E.; Yoshida, H.; Kawai, F.; Shibayama, N.; Kawaguchi, A.; Nagata, K.; Tame, J.R.; Park, S.Y.
The structural basis for an essential subunit interaction in influenza virus RNA polymerase (2008), Nature, 454, 1127-1131.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged subunits PA and PB1 in Escherichia coli	influenza A virus

Crystallization (Commentary)

Crystallization (Comment)	Organism
a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution	influenza A virus

Crystallization (Comment)

Organism

a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution

influenza A virus

Protein Variants

Protein Variants	Comment	Organism
L640D	the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme	influenza A virus
L666D	the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme	influenza A virus
V636S	the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme	influenza A virus
W706A	the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme	influenza A virus

Organism

Organism	UniProt	Comment	Textmining
influenza A virus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged subunits PA and PB1 from Escherichia coli by nickel affinity chromatography	influenza A virus

Subunits

Subunits	Comment	Organism
heterotrimer	the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for virla replication, overview	influenza A virus

Synonyms

Synonyms	Comment	Organism
RNA polymerase	-	influenza A virus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	influenza A virus