Crystal structures of type IIIH NAD-dependent D-3-phosphoglycerate dehydrogenase from two thermophiles

Kumar, S. M. and Pampa, K. J. and Manjula, M. and Hemantha Kumar, G. and Kunishima, N. and Lokanath, N. K. (2014) Crystal structures of type IIIH NAD-dependent D-3-phosphoglycerate dehydrogenase from two thermophiles. Biochemical and Biophysical Research Communications, 451 (1). pp. 126-130. ISSN 0006-291X

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Official URL: https://doi.org/10.1016/j.bbrc.2014.07.075

Abstract

In the l-Serine biosynthesis, D-3-phosphoglycerate dehydrogenase (PGDH) catalyzes the inter-conversion of D-3-phosphoglycerate to phosphohydroxypyruvate. PGDH belongs to 2-hydroxyacid dehydrogenases family. We have determined the crystal structures of PGDH from Sulfolobus tokodaii (StPGDH) and Pyrococcus horikoshii (PhPGDH) using X-ray diffraction to resolution of 1.77 à and 1.95 à , respectively. The PGDH protomer from both species exhibits identical structures, consisting of substrate binding domain and nucleotide binding domain. The residues and water molecules interacting with the NAD are identified. The catalytic triad residues Glu-His-Arg are highly conserved. The residues involved in the dimer interface and the structural features responsible for thermostability are evaluated. Overall, structures of PGDHs with two domains and histidine at the active site are categorized as type IIIH and such PGDHs structures having this type are reported for the first time. © 2014 Elsevier Inc. All rights reserved.

Item Type: Article
Uncontrolled Keywords: nonhuman, X ray diffraction, chemical structure, chemistry, metabolism, priority journal, genetics, Catalytic Domain, enzyme active site, enzymology, crystal structure, Crystallography, water, X ray crystallography, X-Ray, article, protein protein interaction, catalyst, protein motif, protein structure, enzyme stability, Enzyme Stability, protein multimerization, Protein Multimerization, sequence alignment, thermostability, Models, Molecular, binding site, Protein Conformation, Binding Sites, protein conformation, Pyrococcus horikoshii, archaeal protein, Archaeal Proteins, arginine, consensus sequence, glutamic acid, histidine, NAD, nicotinamide adenine dinucleotide, phosphoglycerate dehydrogenase, Phosphoglycerate Dehydrogenase, polypeptide, Sulfolobus, Sulfolobus tokodaii, thermophile
Subjects: B Life Science > Microbiology
D Physical Science > Physics
D Physical Science > Computer Science
Divisions: Department of > Computer Science
Department of > Microbiology
Department of > Physics
Depositing User: Arshiya Kousar
Date Deposited: 26 Jun 2019 06:43
Last Modified: 26 Jun 2019 06:43
URI: http://eprints.uni-mysore.ac.in/id/eprint/3679

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