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

Denessiouk, Jukka Lehtonen, Korpela, Mark S Johnson

Tutkimustuotos: LehtiartikkeliArtikkeliTieteellinenvertaisarvioitu

21 Sitaatiot (Scopus)


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.
AlkuperäiskieliEi tiedossa
JulkaisuProtein Science
DOI - pysyväislinkit
TilaJulkaistu - 1998
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu