Enzyme-mononucleotide interactions: Three different folds share common structural elements for ATP recognition

Protein Science

Volumn 7, Issue 8, 1998, Pages 1768-1771

  Denessiouk, Konstantin A ^a,b,c   Lehtonen, Jukka V ^a,b   Johnson, Mark S ^a,b  

^a ÅBO AKADEMI UNIVERSITY   (Finland)

^b UNIVERSITY OF TURKU   (Finland)

^c MOSCOW INSTITUTE OF PHYSICS AND TECHNOLOGY   (Russian Federation)

Author keywords

Allosteric effector binding site; ATP dependent enzymes; Convergent structural similarities; Local structural comparisons; Similar ligand binding sites

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYCLIC AMP DEPENDENT PROTEIN KINASE; LIGASE; PHOSPHATE; RIBONUCLEOTIDE REDUCTASE;

ALLOSTERISM; ARTICLE; COMPUTER PROGRAM; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; LIGAND BINDING; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ANALYSIS;

EID: 0032464920     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070811     Document Type: Article

References (3)

1. Artymiuk PJ, Poirrette AR, Rice DW, Willett P. 1996. Biotin carboxylase comes into the fold. Nature Struct Biol 3:128-132.
2. Bernstein FC, Koetzle TF, Williams GJB, Meyer EJ, Jr, Brice MD, Rodgers JK, Kennard O, Shimanouchi I, Tasumi M. 1977. The Protein Data Bank: A computer-based archival file for macromolecular structures. J Mol Biol 112:535-542.
3. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J 12:849-859.