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. 1998 May;7(5):1136-46.
doi: 10.1002/pro.5560070507.

Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites

K A Denessiouk  1 , J V Lehtonen, T Korpela, M S Johnson
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Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites

K A Denessiouk et al. Protein Sci. 1998 May.

Abstract

Two proteins, D-alanine:D-alanine ligase and cAMP-dependent protein kinase, share a remarkable degree of structural convergence despite having different three-dimensional folds and different enzymatic functions. Here we report that as many as 103 residues from 10 segments form two identical super-secondary structures between which the cofactor ATP is bound. The cofactor, two bound metal cations, and several water molecules form a large network of electrostatic and hydrophobic interactions common to both enzymes, and these are mediated by the similar placement of equivalent amino acids within the common supersecondary structures.

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