Gerd Schluckebier

TL;DR: The comparable protein folding and the existence of equivalent amino acids in similar secondary and tertiary positions indicate that many (if not all) AdoMet-dependent methyltransferases have a common catalytic domain structure, which permits tertiary structure prediction of other DNA, RNA, protein, and small-molecule Ado metases from their amino acid sequences.

TL;DR: It is proposed that ThT binds in cavities running parallel to the fibril axis, e.g., between the protofilaments forming the fbrils, which have been proposed previously in insulin fibrils and several other amyloid fibrIL models.

TL;DR: The Thermus aquaticus DNA methyltransferase M.Taq I methylates N6 of adenine in the specific double-helical DNA sequence TCGA by transfer of --CH3 from the cofactor S-adenosyl-L-methionine by x-ray crystal structure shows alpha/beta folding of the polypeptide into two domains of about equal size.

TL;DR: Structural comparison of these binary complexes with the complex formed by M.TaqI and the cofactor S-adenosyl-L-methionine suggests that the key element for molecular recognition of these ligands is the binding of their adenosine part in a pocket, and discrimination between cofactor, reaction product and inhibitor is mediated by different conformations of these molecules.

TL;DR: The crystal structure of ErmC' (a naturally occurring variant of ErMC) from Bacillus subtilis has been determined at 3.0 A resolution and a model of SAM bound to Erm C' is presented which is consistent with the motif conservation among MTases.