1hl9
From Proteopedia
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|PDB= 1hl9 |SIZE=350|CAPTION= <scene name='initialview01'>1hl9</scene>, resolution 2.25Å | |PDB= 1hl9 |SIZE=350|CAPTION= <scene name='initialview01'>1hl9</scene>, resolution 2.25Å | ||
|SITE= <scene name='pdbsite=AC1:Fuf+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fuf+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FUF:2-DEOXY-2-FLUORO-BETA-L-FUCOPYRANOSE'>FUF</scene> | + | |LIGAND= <scene name='pdbligand=FUF:2-DEOXY-2-FLUORO-BETA-L-FUCOPYRANOSE'>FUF</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-L-fucosidase Alpha-L-fucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.51 3.2.1.51] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-L-fucosidase Alpha-L-fucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.51 3.2.1.51] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl9 OCA], [http://www.ebi.ac.uk/pdbsum/1hl9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hl9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Henrissat, B.]] | [[Category: Henrissat, B.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
| - | [[Category: FUF]] | ||
[[Category: alpha-l-fucosidase]] | [[Category: alpha-l-fucosidase]] | ||
[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:08 2008'' |
Revision as of 18:07, 30 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Alpha-L-fucosidase, with EC number 3.2.1.51 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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, coupled with kinetic and mutagenesis studies, allowed us to identify the catalytic nucleophile, Asp(244), and the Bronsted acid/base, Glu(266). Because T. maritima alpha-l-fucosidase occupies a unique evolutionary position, being far more closely related to the mammalian enzymes than to any other prokaryotic homolog, a structural model of the human enzyme was built to document the structural consequences of the genetic mutations associated with fucosidosis.
About this Structure
1HL9 is a Single protein structure of sequence from Thermotoga maritima. 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
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