1up6

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{{STRUCTURE_1up6| PDB=1up6 | SCENE= }}
{{STRUCTURE_1up6| PDB=1up6 | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15237973 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15237973}}
==About this Structure==
==About this Structure==
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[[Category: Family4 hydrolase]]
[[Category: Family4 hydrolase]]
[[Category: Nad dependent]]
[[Category: Nad dependent]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:31:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:40:33 2008''

Revision as of 02:40, 28 July 2008

Image:1up6.png

Template:STRUCTURE 1up6

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

Template:ABSTRACT PUBMED 15237973

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 Mon Jul 28 05:40:33 2008

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