4J28: Crystal Structure of a Gh29 Alpha-l-fucosidase Gh29 From Bacteroides Thetaiotaomicron in Complex With a 5-membered Iminocyclitol Inhibitor

Citation:
Abstract
Fucosidases, enzymes that cleave fucose from the non-reducing end of a glycan, represent promising medicinal targets reflecting their roles in cancer metastasis, inflammation, host-parasite interactions and the lysosomal storage disorder fucosidosis. The X-ray crystal structures of Bacteroides thetaiotaomicron GH29 alpha-l-fucosidase (BtFuc2970) in a new crystal form (at a resolution of 1.59A) and liganded with a 5-membered iminocyclitol inhibitor (1.73A) are reported herein. The 5-membered iminocyclitol binds in a (3)E conformation, mimicking the proposed (3)H4 half chair transition-state of the enzyme catalysed reaction, and its Ki for BtFuc2970 was determined as 2muM. Structural analysis of fucosidase inhibition through 5-membered iminocyclitols will aid in the rational design of more potent fucosidase inhibitors for treatment of a range of medical conditions.
PDB ID: 4J28Download
MMDB ID: 109910
PDB Deposition Date: 2013/2/4
Updated in MMDB: 2013/08 
Experimental Method:
x-ray diffraction
Resolution: 1.73  Å
Source Organism:
Similar Structures:
Biological Unit for 4J28: monomeric; determined by author
Molecular Components in 4J28
Label Count Molecule
Protein (1 molecule)
1
Alpha-l-fucosidase
Molecule annotation
Chemicals (10 molecules)
1
1
2
5
3
3
4
1
* Click molecule labels to explore molecular sequence information.

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