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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Cui Z,Li Y,Xiao Y,Feng Y,Cui Qdoi
10.1007/s12104-012-9381-2subject
Has Abstractpub_date
2013-04-01 00:00:00pages
73-6issue
1eissn
1874-2718issn
1874-270Xjournal_volume
7pub_type
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