Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae
Artikel i vetenskaplig tidskrift, 2020

Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in Flavobacterium johnsoniae, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the F. johnsoniae chitobiase (FjGH20) and chitinase B (FjChiB). FjGH20 is a multi-domain enzyme with a helical domain not before observed in other chitobiases and a domain organization reminiscent of GH84 (beta -N-acetylglucosaminidase) family members. The structure of FjChiB reveals that the protein lacks loops and regions associated with exo-acting activity in other chitinases and instead has a more solvent accessible substrate binding cleft, which is consistent with its endo-chitinase activity. Additionally, small angle X-ray scattering data were collected for the internal 70 kDa region that connects the N- and C-terminal chitinase domains of the unique 158 kDa multi-domain chitinase A (FjChiA). The resulting model of the molecular envelope supports bioinformatic predictions of the region comprising six domains, each with similarities to either Fn3-like or Ig-like domains. Taken together, the results provide insights into chitin utilization by F. johnsoniae and reveal structural diversity in bacterial chitin metabolism.


Scott Mazurkewich

Chalmers, Biologi och bioteknik, Industriell bioteknik

Ronny Helland

Universitetet i Tromsø – Norges arktiske universitet

Alasdair Mackenzie

Norges miljø- og biovitenskapelige universitet

Vincent G. H. Eijsink

Norges miljø- og biovitenskapelige universitet

Phillip B. Pope

Norges miljø- og biovitenskapelige universitet

Gisela Branden

Göteborgs universitet

Johan Larsbrink

Chalmers, Biologi och bioteknik, Industriell bioteknik

Scientific Reports

2045-2322 (ISSN)

Vol. 10 1 13775


Biokemi och molekylärbiologi


Biokatalys och enzymteknik





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