5wjp

Crystal structure of the cyclohexadienyl dehydratase-like solute-binding protein SAR11_1068 from Candidatus Pelagibacter ubique.

spinqualitylabelsall models 5wjp, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wjp is a 1 chain structure with sequence from Candidatus Pelagibacter ubique HTCC1062. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4FLR5_PELUB Publication Abstract from PubMed The emergence of enzymes through the neofunctionalization of noncatalytic proteins is ultimately responsible for the extraordinary range of biological catalysts observed in nature. Although the evolution of some enzymes from binding proteins can be inferred by homology, we have a limited understanding of the nature of the biochemical and biophysical adaptations along these evolutionary trajectories and the sequence in which they occurred. Here we reconstructed and characterized evolutionary intermediate states linking an ancestral solute-binding protein to the extant enzyme cyclohexadienyl dehydratase. We show how the intrinsic reactivity of a desolvated general acid was harnessed by a series of mutations radiating from the active site, which optimized enzyme-substrate complementarity and transition-state stabilization and minimized sampling of noncatalytic conformations. Our work reveals the molecular evolutionary processes that underlie the emergence of enzymes de novo, which are notably mirrored by recent examples of computational enzyme design and directed evolution. Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.,Clifton BE, Kaczmarski JA, Carr PD, Gerth ML, Tokuriki N, Jackson CJ Nat Chem Biol. 2018 Apr 23. pii: 10.1038/s41589-018-0043-2. doi:, 10.1038/s41589-018-0043-2. PMID:29686357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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