4E5P

Thermostable phosphite dehydrogenase A176R variant in complex with NAD

Summary for 4E5P

• Entry DOI: 10.2210/pdb4e5p/pdb
• Related: 4E5K 4E5M 4E5N
• Descriptor: Thermostable phosphite dehydrogenase A176R variant, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: d-2-hydroxyacid dehydrogenase, oxidoreductase
• Biological source: Pseudomonas stutzeri
• Total number of polymer chains: 6
• Total formula weight: 221496.91

Authors

Zou, Y.,Zhang, H.,Nair, S.K. (deposition date: 2012-03-14, release date: 2012-05-30, Last modification date: 2024-04-03)

Primary citation

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.
Biochemistry, 51:4263-4270, 2012

PubMed Abstract: The enzyme phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent conversion of phosphite to phosphate and represents the first biological catalyst that has been shown to conduct the enzymatic oxidation of phosphorus. Despite investigation for more than a decade into both the mechanism of its unusual reaction and its utility in cofactor regeneration, there has been a lack of any structural data for PTDH. Here we present the cocrystal structure of an engineered thermostable variant of PTDH bound to NAD(+) (1.7 Å resolution), as well as four other cocrystal structures of thermostable PTDH and its variants with different ligands (all between 1.85 and 2.3 Å resolution). These structures provide a molecular framework for understanding prior mutational analysis and point to additional residues, located in the active site, that may contribute to the enzymatic activity of this highly unusual catalyst.

PubMed: 22564171
DOI: 10.1021/bi2016926

Experimental method

X-RAY DIFFRACTION (1.9 Å)