5od1 | pdb_00005od1

Structure of the engineered metalloesterase MID1sc10 complexed with a phosphonate transition state analogue

spinqualitylabelsall models 5od1, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5od1 is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.34Å Ligands: 9RQ, GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency (k cat/K M ~ 10(6) M(-1) s(-1)). The simultaneous optimization of structure and function in a naive peptide scaffold not only illustrates a plausible enzyme evolutionary pathway from the distant past to the present but also proffers exciting future opportunities for enzyme design and engineering. Evolution of a highly active and enantiospecific metalloenzyme from short peptides.,Studer S, Hansen DA, Pianowski ZL, Mittl PRE, Debon A, Guffy SL, Der BS, Kuhlman B, Hilvert D Science. 2018 Dec 14;362(6420):1285-1288. doi: 10.1126/science.aau3744. PMID:30545884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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