title: Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824.
abstract: Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond these groups and emanate from a branching point between the type I and type III cohesins. Cohesins and dockerins from C. acetobutylicum show low sequence homology to those from other cellulolytic bacteria, and their interactions are specific in corresponding species. Therefore the interactions between cohesins and dockerins from C. acetobutylicum are meaningful to the studies of both cellulosome assembling mechanism and the construction of designer cellulosome. Here we report the NMR resonance assignments of one cohesin from cellulosome scaffoldin cipA and one dockerin from a cellulosomal glycoside hydrolase (family 9) of C. acetobutylicum for further structural determination and functional studies.
authors.affiliation: Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, No. 189 Songling Road, Qingdao, 266101, China.
authors.forename: Zhenling
authors.initials: Z
authors.lastname: Cui
authors.forename: Yifei
authors.initials: Y
authors.lastname: Li
authors.forename: Yan
authors.initials: Y
authors.lastname: Xiao
authors.forename: Yingang
authors.initials: Y
authors.lastname: Feng
authors.forename: Qiu
authors.initials: Q
authors.lastname: Cui
authors.forename: Qui
authors.initials: Q
authors.lastname: Cui
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D044603:Cellulosomes / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry*; D046969:Clostridium acetobutylicum / Q000166:cytology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D000097722:Cohesins
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D000097722:Cohesins