2ZOX

Crystal Structure of the Covalent Intermediate of Human Cytosolic beta-Glucosidase

Summary for 2ZOX

• Entry DOI: 10.2210/pdb2zox/pdb
• Related: 2E9L 2E9M
• Descriptor: Cytosolic beta-glucosidase, alpha-D-glucopyranose, 4-nitrophenyl alpha-D-glucopyranoside, ... (9 entities in total)
• Functional Keywords: hydrolase, glycosidase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytosol: Q9H227
• Total number of polymer chains: 1
• Total formula weight: 55262.79

Authors

Noguchi, J.,Hayashi, Y.,Baba, Y.,Okino, N.,Kimura, M.,Ito, M.,Kakuta, Y. (deposition date: 2008-06-17, release date: 2008-09-30, Last modification date: 2024-10-30)

Primary citation

Noguchi, J.,Hayashi, Y.,Baba, Y.,Okino, N.,Kimura, M.,Ito, M.,Kakuta, Y.
Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase
Biochem.Biophys.Res.Commun., 374:549-552, 2008

PubMed Abstract: Human cytosolic beta-glucosidase, also known as klotho-related protein (KLrP, GBA3), is an enzyme that hydrolyzes various beta-D-glucosides, including glucosylceramide. We recently reported the crystal structure of KLrP in complex with glucose [Y. Hayashi, N. Okino, Y. Kakuta, T. Shikanai, M. Tani, H. Narimatsu, M. Ito, Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase, J. Biol. Chem. 282 (2007) 30889-30900]. Here, we report the crystal structure of a covalent intermediate of the KLrP mutant E165Q, in which glucose was covalently bound to a nucleophile, Glu(373). The structure confirms the double displacement mechanism of the retaining beta-glucosidase. In addition, the structure suggests that a water molecule could be involved in the stabilization of transition states through a sugar, 2-hydroxyl.

PubMed: 18662675
DOI: 10.1016/j.bbrc.2008.07.089

Experimental method

X-RAY DIFFRACTION (1.9 Å)