Literature summary for 1.20.1.1 extracted from

Zou, Y.; Zhang, H.; Brunzelle, J.S.; Johannes, T.W.; Woodyer, R.; Hung, J.E.; Nair, N.; van der Donk, W.A.; Zhao, H.; Nair, S.K.
Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration (2012), Biochemistry, 51, 4263-4270.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas stutzeri

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77	Pseudomonas stutzeri

Crystallization (Comment)

Organism

mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77

Pseudomonas stutzeri

Protein Variants

Protein Variants	Comment	Organism
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D	thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity	Pseudomonas stutzeri

Inhibitors

Inhibitors	Comment	Organism	Structure
sulfite	competitive, cocrystal structure	Pseudomonas stutzeri

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas stutzeri	O69054	-	-

Synonyms

Synonyms	Comment	Organism
PTDH	-	Pseudomonas stutzeri