Literature summary for 2.7.7.19 extracted from

Yang, Q.; Faucher, F.; Coseno, M.; Heckman, J.; Doublie, S.
Purification, crystallization and preliminary X-ray diffraction of a disulfide cross-linked complex between bovine poly(A) polymerase and a chemically modified 15-mer oligo(A) RNA (2011), Acta Crystallogr. Sect. F, 67, 241-244.

Search for more literature for 2.7.7.19

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli Rosetta (DE3) pLysS cells	Bos taurus

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V in complex with a chemically modified RNA, to 2.25 A resolution	Bos taurus

Protein Variants

Protein Variants	Comment	Organism
C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V	introduction of a Cys residue in a mutant lacking all endogenous Cys residues. Mutant achieves maximum specific disulfide cross-linking efficiency. The resulting construct is active and, when mixed with a chemically modified RNA, yields crystals of an enzyme-RNA complex	Bos taurus
C36S/C118V/C160S/C197S/C257S/C293S/C204V	mutation of all seven endogenous cysteine residues. Mutant is able to bind RNA at a level similar to that of wild-type, but no longer forms nonspecific disulfide cross-links with the modified RNA	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P25500	-	-

Synonyms

Synonyms	Comment	Organism
PAP	-	Bos taurus

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Release 2023.1 (January 2023)