6wfh

Streptomyces coelicolor methylmalonyl-CoA epimerase substrate complex

spinqualitylabelsall models 6wfh, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6wfh is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: CL, CO, PEG, SO4, V0V Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9L2C2_STRCO Publication Abstract from PubMed Methylmalonyl-CoA epimerase (MMCE) is proposed to use general acid-base catalysis, but the proposed catalytic glutamic acids are highly asymmetrical in the active site unlike many other racemases. To gain insight into the puzzling relationships between catalytic mechanism, structure, and substrate preference, we solved Streptomyces coelicolor MMCE structures with substrate or 2-nitropropionyl-CoA, an intermediate/transition state analogue. Both ligand bound structures have a planar methylmalonate/2-nitropropionyl moiety indicating a deprotonated C2 with >/=4 A distances to either catalytic acid. Both glutamates interact with the carboxylate/nitro group, either directly or through other residues. This suggests the proposed catalytic acids sequentially catalyze proton shifts between C2 and carboxylate of the substrate with an enolate intermediate. In addition, our structures provide a platform to design mutations for expanding substrate scope to support combinatorial biosynthesis. Substrate Enolate Intermediate and Mimic Captured in the Active Site of Streptomyces coelicolor Methylmalonyl-CoA Epimerase*.,Stunkard LM, Benjamin AB, Bower JB, Huth TJ, Lohman JR Chembiochem. 2021 Dec 1. doi: 10.1002/cbic.202100487. PMID:34856049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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