Sammanfattning

Here we describe the first crystal structure of a beta-1,4-endoglucanase from a brown-rot fungus, Gloeophyllum trabeum GtCel45A, which belongs to subfamily C of glycoside hydrolase family 45 (GH45). GtCel45A is similar to 18 kDa in size and the crystal structure contains 179 amino acids. The structure is refined at 1.30 angstrom resolution and R-free 0.18. The enzyme consists of a single catalytic module folded into a six-stranded double-psi beta-barrel domain surrounded by long loops. GtCel45A is very similar in sequence (82% identity) and structure to PcCel45A from the white-rot fungus Phanerochaete chrysosporium. Surprisingly though, initial hydrolysis of barley beta-glucan was almost twice as fast in GtCel45A as compared to PcCel45A.

Nyckelord

Cel45A; cellulase; cellulose; endoglucanase; glycoside hydrolase GH45

Publicerad i

FEBS open bio
2024, Volym: 14, nummer: 3, sidor: 505-514
Utgivare: WILEY

SLU författare

• Okmane, Laura

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

• Fitkin, Louise

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

• Sandgren, Mats

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

• Ståhlberg, Jerry

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Strukturbiologi
Biokemi och molekylärbiologi


Publikationens identifierare

DOI: https://doi.org/10.1002/2211-5463.13774

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/128668