Structure of Archaeal Glyoxylate Reductase from Pyrococcus Horikoshii Ot3 Complexed with Nicotinamide Adenine Dinucleotide Phosphate.
From: Protein Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan.
Acta crystallographica. Section D, Biological crystallography
- Publish Date: Mar 2007
- ISSN: 0907-4449
- Volume: 63
- Issue: Pt 3
- Pages: 357-65
- Medium: Print
- Language: English
- Citation (JAMA): Yoshikawa Seiko, Arai Ryoichi, Kinoshita Yukiko, et al. Structure of Archaeal Glyoxylate Reductase from Pyrococcus Horikoshii Ot3 Complexed with Nicotinamide Adenine Dinucleotide Phosphate.. Acta Crystallogr. D Biol. Crystallogr. Mar 2007;63:357-65
Abstract
Glyoxylate reductase catalyzes the NAD(P)H-linked reduction of glyoxylate to glycolate. Here, the 1.7 A crystal structure of glyoxylate reductase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate [NADP(H)] determined by the single-wavelength anomalous dispersion (SAD) method is reported. The monomeric structure comprises the two domains typical of NAD(P)-dependent dehydrogenases: the substrate-binding domain (SBD) and the nucleotide-binding domain (NBD). The crystal structure and analytical ultracentrifugation results revealed dimer formation. In the NADP(H)-binding site, the pyrophosphate moiety and the 2’-phosphoadenosine moiety are recognized by the glycine-rich loop (residues 157-162) and by loop residues 180-182, respectively. Furthermore, the present study revealed that P. horikoshii glyoxylate reductase contains aromatic clusters and has a larger number of ion pairs and a lower percentage of hydrophobic accessible surface area than its mesophilic homologues, suggesting its thermostability mechanism.
Mesh Headings (Keywords): Alcohol Oxidoreductases, Amino Acid Sequence, Archaeal Proteins, Binding Sites, Dimerization, Molecular Sequence Data, NADP, Protein Conformation, Protein Structure, Tertiary, Pyrococcus horikoshii, Sequence Alignment
Check for Full Text / PubMed Unique Identifier (PMID): 17327673
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