6YHH
X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20)
Summary for 6YHH
Entry DOI | 10.2210/pdb6yhh/pdb |
Descriptor | Beta-N-acetylglucosaminidase-like protein Glycoside hydrolase family 20, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (4 entities in total) |
Functional Keywords | bacterial chitin metabolism, chitin degradation, n-acetylglucosaminidase, gh20, hydrolase |
Biological source | Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) |
Total number of polymer chains | 2 |
Total formula weight | 151828.77 |
Authors | Mazurkewich, S.,Helland, R.,MacKenzie, A.,Eijsink, V.G.H.,Pope, P.B.,Branden, G.,Larsbrink, J. (deposition date: 2020-03-30, release date: 2020-09-02, Last modification date: 2024-01-24) |
Primary citation | Mazurkewich, S.,Helland, R.,Mackenzie, A.,Eijsink, V.G.H.,Pope, P.B.,Branden, G.,Larsbrink, J. Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae. Sci Rep, 10:13775-13775, 2020 Cited by PubMed Abstract: 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 (β-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. PubMed: 32792608DOI: 10.1038/s41598-020-70749-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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