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

Denessiouk, Jukka Lehtonen, Korpela, Mark S Johnson

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

21 Citeringar (Scopus)

Sammanfattning

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.
OriginalspråkOdefinierat/okänt
Sidor (från-till)1136–1146
TidskriftProtein Science
Volym7
Utgåva5
DOI
StatusPublicerad - 1998
MoE-publikationstypA1 Tidskriftsartikel-refererad

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