8adq

Crystal structure of holo-SwHPA-Mg (hydroxy ketone aldolase) from Sphingomonas wittichii RW1 in complex with hydroxypyruvate and D-Glyceraldehyde

spinqualitylabelsall models 8adq, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8adq is a 1 chain structure with sequence from Rhizorhabdus wittichii RW1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: 3GR, 3PY, BR, K, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 ( Sw HKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M 2+ R ), 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 2+ A ) at 2.4 A distance. Bidentate coordination of a ketoacid substrate to M 2+ A affords the overall lowest energy complex, which drives the transition from M 2+ R to M 2+ A . 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. Substrate Induced Movement of the Metal Cofactor between Active and Resting State.,Marsden SR, Wijma HJ, Mohr MKF, Justo I, Hagedoorn PL, Laustsen J, Jeffries CM, Svergun D, Mestrom L, McMillan DGG, Bento I, Hanefeld U Angew Chem Int Ed Engl. 2022 Oct 10. doi: 10.1002/anie.202213338. PMID:36214476 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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