3ASV
The Closed form of serine dehydrogenase complexed with NADP+
Summary for 3ASV
| Entry DOI | 10.2210/pdb3asv/pdb |
| Related | 3ASU |
| Descriptor | Short-chain dehydrogenase/reductase SDR, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | sdr family, rossmann fold, short-chain dehydrogenase/reductase, l-allo-threonine dehydrogenase, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 168697.58 |
| Authors | Yamazawa, R.,Nakajima, Y.,Yoshimoto, T.,Ito, K. (deposition date: 2010-12-21, release date: 2011-10-12, Last modification date: 2023-11-01) |
| Primary citation | Yamazawa, R.,Nakajima, Y.,Mushiake, K.,Yoshimoto, T.,Ito, K. Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation. J.Biochem., 149:701-712, 2011 Cited by PubMed Abstract: Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. The enzyme shows a stereospecificity for β-(3S)-hydroxy acid as a substrate; however, no stereospecificity was observed at the α-carbon. The structures of the ligand-free SerDH and SerDH-NADP(+)-phosphate complex were determined at 1.9 and 2.7 Å resolutions, respectively. The overall structure, including the catalytic tetrad of Asn106, Ser134, Tyr147 and Lys151, shows obvious relationships with other members of the SDR family. The structure of the substrate-binding loop and that of the C-terminal region were disordered in the ligand-free enzyme, whereas these structures were clearly defined in the SerDH-NADP(+) complex as a closed form. Interestingly, the C-terminal region was protruded from the main body and it formed an anti-parallel β-sheet with another C-terminal region on the subunit that is diagonally opposite to that in the tetramer. It is revealed that the C-terminal region possesses the important roles in substrate binding through the stabilization of the substrate-binding loop in the closed form complex. The roles of the C-terminal region along with those of the residues involved in substrate recognition were studied by site-directed mutagenesis. PubMed: 21349860DOI: 10.1093/jb/mvr024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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