Characterization of the cofactor-binding site in the SPOUT-fold methyltransferases by computational docking of S-adenosylmethionine to three crystal structures.

ABSTRACT: BACKGROUND:There are several evolutionarily unrelated and structurally dissimilar superfamilies of S-adenosylmethionine (AdoMet)-dependent methyltransferases (MTases). A new superfamily (SPOUT) has been recently characterized on a sequence level and three structures of its members (1gz0, 1ipa, and 1k3r) have been solved. However, none of these structures include the cofactor or the substrate. Due to the strong evolutionary divergence and the paucity of experimental information, no confident predictions of protein-ligand and protein-substrate interactions could be made, which hampered the study of sequence-structure-function relationships in the SPOUT superfamily. RESULTS:We used the computational docking program AutoDock to identify the AdoMet-binding site on the surface of three MTase str

SUBMITTER: Kurowski MA 

PROVIDER: S-EPMC153507 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature