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Two “unrelated” families of ATP‐dependent enzymes share extensive structural similarities about their cofactor binding sites
Author(s) -
Denessiouk Konstantin A.,
Korpela Timo,
Lehtonen Jukka V.,
Johnson Mark S.
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070507
Subject(s) - cofactor , enzyme , dna ligase , alanine , biochemistry , chemistry , protein structure , amino acid , transferase , stereochemistry , biology
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.