SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)
Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
Secondary Structure and Calcium-induced Folding of the Clostridium thermocellum Dockerin Domain Determined by NMR Spectroscopy
Involvement of Both Dockerin Subdomains in Assembly of the Clostridium thermocellum Cellulosome
TYPE I DOCKERIN DOMAIN (RESIDUES 673-741)
HELIX DETERMINATION METHOD: AUTHOR-DETERMINED
THIS STRUCTURE WAS DETERMINED BY STANDARD TECHNIQUES USING UNLABELED AND 15N- LABELED DOCKERIN.
THE STRUCTURE IS BASED ON 728 NOE-DERIVED DISTANCE CONSTRAINTS, 79 DIHEDRAL ANGLE CONSTRAINTS, AND 12 CALCIUM ION RESTRAINTS.
100MM POTASSIUM CHLORIDE; 20MM CALCIUM CHLORIDE; 90% H2O, 10% D2O
F. DELAGALIO, S. GRZESIEK, G. VUISTER, G. ZHU, J. PFEIFER, A. BAX
CELLULOSE DEGRADATION, CELLULOSOME, CALCIUM-BINDING, HYDROLASE