Literature summary for 2.4.2.1 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 2.4.2.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the wild-type and a C-terminal KH/S1 domain-truncated mutant of PNPase at resolutions of 2.6 A and 2.8 A, respectively	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	the C-terminal KH/S1 domain-truncated mutant binds and cleaves RNA less efficiently with an eightfold reduced binding affinity. The mutant forms a less stable trimer than the full-length PNPase. The crystal structure of DeltaKH/S1 is more expanded, containing a slightly wider central channel than that of the wild-type PNPase, suggesting that the KH/S1 domain helps PNPase to assemble into a more compact trimer, and it regulates the channel size allosterically	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
PNPase	-	Escherichia coli

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Release 2023.1 (January 2023)