9eia

A broad-substrate spectrum lactate racemase A from Isosphaera pallida in complex with copurified D-lactate

spinqualitylabelsall models 9eia, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9eia is a 2 chain structure with sequence from Isosphaera pallida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.74Å Ligands: 4EY, EDO, LAC, NI, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E8QWZ4_ISOPI Publication Abstract from PubMed The LarA family consists of diverse racemases/epimerases that interconvert the diastereomers of a variety of alpha-hydroxyacids by using a nickel-pincer nucleotide (NPN) cofactor. The hidden redox reaction catalyzed by the NPN cofactor makes LarA enzymes attractive engineering targets for applications. However, how a LarA enzyme binds its natural substrate and recognizes different alpha-hydroxyacids has not been elucidated. Here, we report three high-resolution structures of the enzyme-substrate complexes of a broad-spectrum LarA enzyme from Isosphaera pallida (LarA (Ip) ). The substrate binding mode reveals an optimal orientation and distance between the hydride donor and acceptor, strongly supporting the proposed proton-coupled hydride transfer mechanism. The experimentally solved structures, together with the structural models of other LarA enzymes, allow us to identify the residues/structural elements critically involved in the interactions with different alpha-hydroxyacid substrates. Collectively, this work provides a critical structural basis for catalysis and substrate recognition of the diverse enzymes in the LarA family, thus building a foundation for enzyme engineering. Structural Basis for Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.,Gatreddi S, Urdiain-Arraiza J, Desguin B, Hausinger RP, Hu J bioRxiv [Preprint]. 2024 Nov 28:2024.11.28.625916. doi: , 10.1101/2024.11.28.625916. PMID:39651260 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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