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1up6
From Proteopedia
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[[Image:1up6.jpg|left|200px]] | [[Image:1up6.jpg|left|200px]] | ||
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'''STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE''' | '''STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE''' | ||
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==Reference== | ==Reference== | ||
An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima., Yip VL, Varrot A, Davies GJ, Rajan SS, Yang X, Thompson J, Anderson WF, Withers SG, J Am Chem Soc. 2004 Jul 14;126(27):8354-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15237973 15237973] | An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima., Yip VL, Varrot A, Davies GJ, Rajan SS, Yang X, Thompson J, Anderson WF, Withers SG, J Am Chem Soc. 2004 Jul 14;126(27):8354-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15237973 15237973] | ||
| - | [[Category: Endo-1,3(4)-beta-glucanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: Yip, V L.]] | [[Category: Yip, V L.]] | ||
[[Category: 6-phospho-beta-glucosidase]] | [[Category: 6-phospho-beta-glucosidase]] | ||
| - | [[Category: | + | [[Category: Family4 hydrolase]] |
| - | [[Category: | + | [[Category: Nad dependent]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:31:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:31, 3 May 2008
STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.55 ANGSTROM RESOLUTION IN THE TETRAGONAL FORM WITH MANGANESE, NAD+ AND GLUCOSE-6-PHOSPHATE
Overview
Among the numerous well-characterized families of glycosidases, family 4 appears to be the anomaly, requiring both catalytic NAD+ and a divalent metal for activity. The unusual cofactor requirement prompted the proposal of a mechanism involving key NAD+-mediated redox steps as well as elimination of the glycosidic oxygen. Primary kinetic isotope effects for the 2- and 3-deutero substrate analogues, isotopic exchange with solvent, and structural analysis of a 6-phospho-beta-glucosidase, BglT (E.C. 3.2.1.6), provided evidence in support of the proposed mechanism, which has striking resemblances to that of the sugar dehydratases. Furthermore, analysis of the stereochemical outcome indicated that family 4 enzymes are retaining glycosidases.
About this Structure
1UP6 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima., Yip VL, Varrot A, Davies GJ, Rajan SS, Yang X, Thompson J, Anderson WF, Withers SG, J Am Chem Soc. 2004 Jul 14;126(27):8354-5. PMID:15237973 Page seeded by OCA on Sat May 3 11:31:34 2008
