2m3s

Calmodulin, i85l, f92e, h107i, l112r, a128t, m144r mutantCalmodulin, i85l, f92e, h107i, l112r, a128t, m144r mutant

Structural highlights 2m3s is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CALM_CHICK Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Publication Abstract from PubMed It only takes one mutation: A strategically placed single mutation in a non-enzymatic protein scaffold produced AlleyCat, a small, allosterically regulated catalyst of Kemp elimination. In only seven rounds of directed evolution the enzymatic efficiency of the original 74 amino acid residue catalyst was improved more than 220-fold to achieve a kcat value higher than that of catalytic antibodies for the same reaction, still preserving allosteric regulation. A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction.,Moroz OV, Moroz YS, Wu Y, Olsen AB, Cheng H, Mack KL, McLaughlin JM, Raymond EA, Zhezherya K, Roder H, Korendovych IV Angew Chem Int Ed Engl. 2013 Jun 10;52(24):6246-9. doi: 10.1002/anie.201302339., Epub 2013 Apr 29. PMID:23630096 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Calmodulin 3D structures

spinqualitylabelsall models 2m3s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image