A study into the effects of protein binding on nucleotide conformation.
In this study, we examine the effects of binding to protein upon nucleotide conformation, by the comparison of X-ray crystal structures of free and protein-bound nucleotides. A dataset of structurally non-homologous protein-nucleotide complexes was derived from the Brookhaven Protein Data Bank by a novel protocol of dual sequential and structural alignments, and a dataset of native nucleotide structures was obtained from the Cambridge Structural Database. The nucleotide torsion angles and sugar puckers, which describe nucleotide conformation, were analysed in both datasets and compared. Differences between them are described and discussed. Overall, the nucleotides were found to bind in low energy conformations, not significantly different from their 'free' conformations except that they adopted an extended conformation in preference to the 'closed' structure predominantly observed by free nucleotide. The archetypal conformation of a protein-bound nucleotide is derived from these observations.
Moodie
S L
SL
Department of Biochemistry and Molecular Biology, University College, London, UK.
Thornton
J M
JM
D003461:Crystallography; D066298:In Vitro Techniques; D008958:Models, Molecular; D015394:Molecular Structure; D009711:Nucleotides / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000648:ultrastructure*; D012266:Ribose / Q000737:chemistry
D009711:Nucleotides; D011506:Proteins; D012266:Ribose