6CI9
RMM microcompartment-associated aminopropanol dehydrogenase NADP + aminoacetone holo-structure
Summary for 6CI9
| Entry DOI | 10.2210/pdb6ci9/pdb |
| Descriptor | 3-oxoacyl-[acyl-carrier-protein] reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 1-aminopropan-2-one, ... (6 entities in total) |
| Functional Keywords | dehydrogenase, short-chain dehydrogenase/reductase, oxidoreductase |
| Biological source | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) |
| Total number of polymer chains | 16 |
| Total formula weight | 442517.84 |
| Authors | Mallette, E.,Kimber, M.S. (deposition date: 2018-02-23, release date: 2018-05-30, Last modification date: 2023-10-04) |
| Primary citation | Mallette, E.,Kimber, M.S. Structure and Kinetics of the S-(+)-1-Amino-2-propanol Dehydrogenase from the RMM Microcompartment of Mycobacterium smegmatis. Biochemistry, 57:3780-3789, 2018 Cited by PubMed Abstract: S-(+)-1-Amino-2-propanol dehydrogenase (APDH) is a short-chain dehydrogenase/reductase associated with the incompletely characterized Rhodococcus and Mycobacterium bacterial microcompartment (RMM). We enzymatically characterized the APDH from M. smegmatis and showed it is highly selective, with a low micromolar K for S-(+)-1-amino-2-propanol and specificity for NADP(H). A paralogous enzyme from a nonmicrocompartment-associated operon in the same organism was also shown to have a similar activity. We determined the structure of APDH in both apo form (at 1.7 Å) and as a ternary enzyme complex with NADP and aminoacetone (at 1.9 Å). Recognition of aminoacetone was mediated by strong hydrogen bonds to the amino group by Thr145 and by Glu251 from the C-terminus of an adjacent protomer. The substrate binding site entirely encloses the substrate, with close contacts between the aminoacetone methyl group and Phe95, Trp154, and Leu195. Kinetic characterization of several of these residues confirm their importance in enzyme functioning. Bioinformatics analysis of APDH homologues implies that many nonmicrocompartment APDH orthologues partake in an aminoacetone degradation pathway that proceeds via an aminopropanol O-phosphate phospholyase. RMM microcompartments may mediate a similar pathway, though possibly with differences in the details of the pathway that necessitates encapsulation behind a shell. PubMed: 29757625DOI: 10.1021/acs.biochem.8b00464 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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