Literature summary for 2.7.7.8 extracted from

Shi, Z.; Yang, W.Z.; Lin-Chao, S.; Chak, K.F.; Yuan, H.S.
Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation (2008), RNA, 14, 2361-2371.

Search for more literature for 2.7.7.8

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and C-terminal KH/S1 domain truncated mutant at resolutions of 2.6 and 2.8 A, respectively. The six PH domains assemble into a ring-like structure containing a central channel	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	C-terminal KH/S1 domain truncated mutant, crystallization data. Mutant binds and cleaves RNA less efficiently with an 8fold reduced binding affinity and forms a less stable trimer. Mutation of Arg-residues in the central channel neck region produces defective enzymes that either bind and cleave RNA less efficiently or generate longer cleaved oligonucleotide products	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P05055	-	-

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Release 2023.1 (January 2023)