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1hl9
From Proteopedia
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CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR
Overview
Fucosylated glycoconjugates are involved in numerous biological events, and alpha-l-fucosidases, the enzymes responsible for their processing, are, therefore of crucial importance. Deficiency in alpha-l-fucosidase activity, is associated with fucosidosis, a lysosomal storage disorder characterized, by rapid neurodegeneration, resulting in severe mental and motor, deterioration. To gain insight into alpha-l-fucosidase function at the, molecular level, we have determined the crystal structure of Thermotoga, maritima alpha-l-fucosidase. This enzyme assembles as a hexamer and, displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like, domain and a C-terminal beta-sandwich domain. The structures of an, enzyme-product complex and of a covalent glycosyl-enzyme intermediate, ... [(full description)]
About this Structure
1HL9 is a [Single protein] structure of sequence from [Thermotoga maritima] with FUF as [ligand]. Active as [Alpha-L-fucosidase], with EC number [3.2.1.51]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis., Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y, J Biol Chem. 2004 Mar 26;279(13):13119-28. Epub 2004 Jan 8. PMID:14715651
Page seeded by OCA on Tue Oct 30 15:38:27 2007
