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PDBsum entry 2wc4
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine
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Structure:
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Beta-glucosidase a. Chain: a, b, c, d. Fragment: residues 2-446. Synonym: beta-glucosidase, gentiobiase, cellobiase, beta-d-glucoside glucohydrolase. Engineered: yes
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.70Å
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R-factor:
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0.169
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R-free:
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0.213
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Authors:
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M.Aguilar,T.M.Gloster,J.P.Turkenburg,M.I.Garcia-Moreno,C.Ortiz Mellet,G.J.Davies,J.M.Garcia Fernandez
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Key ref:
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M.Aguilar-Moncayo
et al.
(2009).
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
Org Biomol Chem,
7,
2738-2747.
PubMed id:
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Date:
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08-Mar-09
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Release date:
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14-Apr-09
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PROCHECK
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Headers
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References
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Q08638
(BGLA_THEMA) -
Beta-glucosidase A from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq:
Struc:
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446 a.a.
443 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.2.1.21
- beta-glucosidase.
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Reaction:
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Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
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Org Biomol Chem
7:2738-2747
(2009)
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PubMed id:
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Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
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M.Aguilar-Moncayo,
T.M.Gloster,
J.P.Turkenburg,
M.I.García-Moreno,
C.Ortiz Mellet,
G.J.Davies,
J.M.García Fernández.
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ABSTRACT
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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.
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Links
