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Enzyme‐mononucleotide interactions: Three different folds share common structural elements for atp recognition
Author(s) -
Denessiouk Konstantin A.,
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.5560070811
Subject(s) - stereochemistry , dna ligase , ribonucleotide reductase , biochemistry , enzyme , protein structure , chemistry , protein secondary structure , amino acid , protein subunit , gene
Three ATP‐dependent enzymes with different folds, cAMP‐dependent protein kinase, D‐Ala:D‐Ala ligase and the α‐subunit of the α 2 β 2 ribonucleotide reductase, have a similar organization of their ATP‐binding sites. The most meaningful similarity was found over 23 structurally equivalent residues in each protein and includes three strands each from their β‐sheets, in addition to a connecting loop. The equivalent secondary structure elements in each of these enzymes donate four amino acids forming key hydrogen bonds responsible for the common orientation of the “AMP” moieties of their ATP‐ligands. One lysine residue conserved throughout the three families binds the alpha‐phosphate in each protein. The common fragments of structure also position some, but not all, of the equivalent residues involved in hydrophobic contacts with the adenine ring. These examples of convergent evolution reinforce the view that different proteins can fold in different ways to produce similar structures locally, and nature can take advantage of these features when structure and function demand it, as shown here for the common mode of ATP‐binding by three unrelated proteins.