4BYA

Calmodulin, C-terminal domain, M144H mutant

Summary for 4BYA

• Entry DOI: 10.2210/pdb4bya/pdb
• NMR Information: BMRB: 19376
• Descriptor: CALMODULIN, C-TERMINAL DOMAIN, M144H MUTANT, CALCIUM ION (2 entities in total)
• Functional Keywords: calmodulin, metal binding protein
• Biological source: GALLUS GALLUS (BANTAM, CHICKENS)
• Total number of polymer chains: 1
• Total formula weight: 8703.55

Authors

Moroz, Y.S.,Wu, Y.,van Nuland, N.A.J.,Korendovych, I.V. (deposition date: 2013-07-18, release date: 2014-06-18, Last modification date: 2024-06-19)

Primary citation

Moroz, Y.S.,Dunston, T.T.,Makhlynets, O.V.,Moroz, O.V.,Wu, Y.,Yoon, J.H.,Olsen, A.B.,Mclaughlin, J.M.,Mack, K.L.,Gosavi, P.M.,Van Nuland, N.A.J.,Korendovych, I.V.
New Tricks for Old Proteins: Single Mutations in a Nonenzymatic Protein Give Rise to Various Enzymatic Activities.
J.Am.Chem.Soc., 137:14905-, 2015

PubMed Abstract: Design of a new catalytic function in proteins, apart from its inherent practical value, is important for fundamental understanding of enzymatic activity. Using a computationally inexpensive, minimalistic approach that focuses on introducing a single highly reactive residue into proteins to achieve catalysis we converted a 74-residue-long C-terminal domain of calmodulin into an efficient esterase. The catalytic efficiency of the resulting stereoselective, allosterically regulated catalyst, nicknamed AlleyCatE, is higher than that of any previously reported de novo designed esterases. The simplicity of our design protocol should complement and expand the capabilities of current state-of-art approaches to protein design. These results show that even a small nonenzymatic protein can efficiently attain catalytic activities in various reactions (Kemp elimination, ester hydrolysis, retroaldol reaction) as a result of a single mutation. In other words, proteins can be just one mutation away from becoming entry points for subsequent evolution.

PubMed: 26555770
DOI: 10.1021/JACS.5B07812

Experimental method

SOLUTION NMR