7OBU
Crystal structure of holo-F210W mutant of Hydroxy ketone aldolase (SwHKA) from Sphingomonas wittichii RW1, with the active site in the resting and the active state
Summary for 7OBU
| Entry DOI | 10.2210/pdb7obu/pdb |
| Related | 6R62 7NNK 7NR1 7NUJ 7O5I 7O5R 7O5V 7O5W 7O87 7O9R |
| Descriptor | HpcH/HpaI aldolase, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | class ii pyruvate aldolase, metal dependent, aldol reaction, hydroxypyruvate, pyruvate, aldolase, carbon bond formation, holo, lyase |
| Biological source | Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273) |
| Total number of polymer chains | 2 |
| Total formula weight | 53877.99 |
| Authors | Laustsen, J.,Justo, I.,Marsden, S.R.,Hanefeld, U.,Bento, I. (deposition date: 2021-04-23, release date: 2022-10-26, Last modification date: 2024-01-31) |
| Primary citation | Marsden, S.R.,Wijma, H.J.,Mohr, M.K.F.,Justo, I.,Hagedoorn, P.L.,Laustsen, J.,Jeffries, C.M.,Svergun, D.,Mestrom, L.,McMillan, D.G.G.,Bento, I.,Hanefeld, U. Substrate Induced Movement of the Metal Cofactor between Active and Resting State. Angew.Chem.Int.Ed.Engl., 61:e202213338-e202213338, 2022 Cited by PubMed Abstract: Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally required to tune the metal cofactor's properties by allosteric regulation. Here structural analysis of hydroxyketoacid aldolase from Sphingomonas wittichii RW1 (SwHKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M ), the metal constitutes an integral part of the dimer interface within the overall hexameric assembly, but sterical constraints do not allow for substrate binding. Conversely, a second coordination sphere constitutes the catalytically active state (M ) at 2.4 Å distance. Bidentate coordination of a ketoacid substrate to M affords the overall lowest energy complex, which drives the transition from M to M . While not described earlier, this type of regulation may be widespread and largely overlooked due to low occupancy of some of its states in protein crystal structures. PubMed: 36214476DOI: 10.1002/anie.202213338 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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