Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermineStructure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine

Structural highlights

2wc3 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BGLA_THEMA

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase.

Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.,Aguilar-Moncayo M, Gloster TM, Turkenburg JP, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Garcia Fernandez JM Org Biomol Chem. 2009 Jul 7;7(13):2738-47. Epub 2009 May 22. PMID:19532990[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Aguilar-Moncayo M, Gloster TM, Turkenburg JP, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Garcia Fernandez JM. Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring. Org Biomol Chem. 2009 Jul 7;7(13):2738-47. Epub 2009 May 22. PMID:19532990 doi:10.1039/b906968b

2wc3, resolution 2.00Å

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