Literature summary for 2.7.7.89 extracted from

Xu, Y.; Wen, D.; Clancy, P.; Carr, P.; Ollis, D.; Vasudevan, S.
Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase (2004), Protein Expr. Purif., 34, 142-146.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of a soluble N-terminal domain, residues 1-440, to 2.6 A resolution	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	expression of soluble N-terminal domain, residues 1-440, of the Escherichia coli adenylyl transferase responsible for deadenylylation activity. The domain is truncated at the end of a predicted helix and prior to a Q-linker, it is very soluble and stable. The construct has deadenylylation activity that is independent of the low nitrogen status indicator PII-UMP	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30870	-	-

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Release 2023.1 (January 2023)