5K1S
crystal structure of AibC
Summary for 5K1S
| Entry DOI | 10.2210/pdb5k1s/pdb |
| Descriptor | Oxidoreductase, zinc-binding dehydrogenase family, ZINC ION (3 entities in total) |
| Functional Keywords | medium chain reductase, isovalerate, hexahistidine tag, tev-protease recognition sequence, oxidoreductase |
| Biological source | Myxococcus xanthus (strain DK 1622) |
| Total number of polymer chains | 4 |
| Total formula weight | 153433.99 |
| Authors | Bock, T.,Mueller, R.,Blankenfeldt, W. (deposition date: 2016-05-18, release date: 2016-08-10, Last modification date: 2024-05-08) |
| Primary citation | Bock, T.,Muller, R.,Blankenfeldt, W. Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. Acta Crystallogr.,Sect.F, 72:652-658, 2016 Cited by PubMed Abstract: Isovaleryl coenzyme A (IV-CoA) performs a crucial role during development and fruiting-body formation in myxobacteria, which is reflected in the existence of a de novo biosynthetic pathway that is highly upregulated when leucine, the common precursor of IV-CoA, is limited. The final step in de novo IV-CoA biosynthesis is catalyzed by AibC, a medium-chain dehydrogenase/reductase. Here, the crystal structure of AibC from Myxococcus xanthus refined to 2.55 Å resolution is presented. The protein adopts two different conformations in the crystal lattice, which is a consequence of partial interaction with the purification tag. Based on this structure, it is suggested that AibC most probably uses a Zn(2+)-supported catalytic mechanism in which NADPH is preferred over NADH. Taken together, this study reveals structural details of the alternative IV-CoA-producing pathway in myxobacteria, which may serve as a base for further biotechnological research and biofuel production. PubMed: 27487931DOI: 10.1107/S2053230X16011146 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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