title: Backbone assignments for the SPOUT methyltransferase MTTTm, a knotted protein from Thermotoga maritima.
abstract: The SPOUT family of methyltransferase proteins is noted for containing a deep trefoil knot in their defining backbone fold. This unique fold is of high interest for furthering the understanding of knots in proteins. Here, we report the1H,13C,15N assignments for MTTTm, a canonical member of the SPOUT family. This protein is unique, as it is one of the smallest members of the family, making it an ideal system for probing the unique properties of the knot. Our present work represents the foundation for further studies into the topology of MTTTm, and understanding how its structure affects both its folding and function.
authors.affiliation: Department of Chemistry and Biochemistry, University of California at San Diego (UCSD), La Jolla, CA, USA.
authors.forename: David J
authors.initials: DJ
authors.lastname: Burban
authors.affiliation: Department of Chemistry and Biochemistry, University of California at San Diego (UCSD), La Jolla, CA, USA. pajennings@ucsd.edu.
authors.forename: Patricia A
authors.initials: PA
authors.lastname: Jennings
mesh_terms: D008780:Methyltransferases / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D020124:Thermotoga maritima / Q000201:enzymology*
chemical_list: D008780:Methyltransferases
keywords: Minimal tied trefoil; SPOUT methyltransferase; Topology; Trefoil knot