1L8F

Structure of 20K-endoglucanase from Melanocarpus albomyces at 1.8 A

Summary for 1L8F

• Entry DOI: 10.2210/pdb1l8f/pdb
• Descriptor: Endoglucanase (2 entities in total)
• Functional Keywords: cellulase, thermophilic, endoglucanase, hydrolase
• Biological source: Melanocarpus albomyces
• Total number of polymer chains: 1
• Total formula weight: 22230.38

Authors

Valjakka, J.,Rouvinen, J. (deposition date: 2002-03-20, release date: 2003-04-01, Last modification date: 2024-10-16)

Primary citation

Valjakka, J.,Rouvinen, J.
Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 A resolution.
Acta Crystallogr.,Sect.D, 59:765-768, 2003

PubMed Abstract: The crystal structure of the 20K endoglucanase from the thermophilic fungus Melanocarpus albomyces (Ma20k) has been determined. The structure was refined to 1.8 A resolution using data obtained at 120 K. Ma20k belongs to glycoside hydrolase family 45. The three-dimensional structures of endoglucanase V (EGV) from the fungus Humicola insolens and of an endoglucanase from H. grisea var. thermoidea have previously been determined. The overall structure of Ma20k consists of a six-stranded beta-barrel domain similar to that found previously in family 45 endoglucanases. The flexible loop between strands V and VI, which was disordered in the uncomplexed structures of the Humicola endoglucanases but was ordered in complexed structures of EGV, is found to be well ordered in the native structure of Ma20k. The structure of Ma20k allows comparison between thermophilic and mesophilic proteins of family 45 and different principles for thermostability are discussed.

PubMed: 12657806
DOI: 10.1107/S0907444903002051

Experimental method

X-RAY DIFFRACTION (1.8 Å)