1qvb

From Proteopedia

Revision as of 02:20, 25 November 2007

CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS

Overview

The glycosyl hydrolases are an important group of enzymes that are, responsible for cleaving a range of biologically significant carbohydrate, compounds. Structural information on these enzymes has provided useful, information on their molecular basis for the functional variations, while, the characterization of the structural features that account for the high, thermostability of proteins is of great scientific and biotechnological, interest. To these ends we have determined the crystal structure of the, beta-glycosidase from a hyperthermophilic archeon Thermosphaera aggregans., The structure is a (beta/alpha)8 barrel (TIM-barrel), as seen in other, glycosyl hydrolase family 1 members, and forms a tetramer. Inspection of, the active site and the surrounding area reveals two catalytic glutamate, residues consistent with the retaining mechanism and the surrounding polar, and aromatic residues consistent with a monosaccharide binding site., Comparison of this structure with its mesophilic counterparts implicates a, variety of structural features that could contribute to the, thermostability. These include an increased number of surface ion pairs, an increased number of internal water molecules and a decreased surface, area upon forming an oligomeric quaternary structure.

About this Structure

1QVB is a Single protein structure of sequence from Thermosphaera aggregans. Full crystallographic information is available from OCA.

Reference

Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability., Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH, FEBS Lett. 1999 Feb 26;445(2-3):375-83. PMID:10094493

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