3WP3

Xylanase 11C from Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus)

Summary for 3WP3

• Entry DOI: 10.2210/pdb3wp3/pdb
• Descriptor: Endo-1,4-beta-xylanase (2 entities in total)
• Functional Keywords: beta-jelly roll, glycoside hydrolase, hydrolase
• Biological source: Talaromyces funiculosus (Fruitlet core rot fungus)
• Cellular location: Secreted : Q9HFH0
• Total number of polymer chains: 2
• Total formula weight: 44990.23

Authors

Ishikawa, K.,Inoue, H.,Kataoka, M. (deposition date: 2014-01-09, release date: 2014-11-26, Last modification date: 2024-03-20)

Primary citation

Kataoka, M.,Akita, F.,Maeno, Y.,Inoue, B.,Inoue, H.,Ishikawa, K.
Crystal structure of Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) GH family 11 xylanase
Appl Biochem Biotechnol., 174:1599-1612, 2014

PubMed Abstract: Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) is one of the mesophilic fungi that can produce high levels of cellulose-related enzymes and are expected to be used for the degradation of polysaccharide biomass. In silico analysis of the genome sequence of T. cellulolyticus detected seven open reading frames (ORFs) showing homology to xylanases from glycoside hydrolase (GH) family 11. The gene encoding the GH11 xylanase C (TcXylC) with the highest activity was used for overproduction and purification of the recombinant enzyme, permitting solving of the crystal structure to a resolution of 1.98 Å. In the asymmetric unit, two kinds of the crystal structures of the xylanase were identified. The main structure of the protein showed a β-jelly roll structure. We hypothesize that one of the two structures represents the open form and the other shows the close form. The changing of the flexible region between the two structures is presumed to induce and accelerate the enzyme reaction. The specificity of xylanase toward the branched xylan is discussed in the context of this structural data and by comparison with the other published structures of xylanases.

PubMed: 25138599
DOI: 10.1007/s12010-014-1130-9

Experimental method

X-RAY DIFFRACTION (1.98 Å)