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1up6

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[[Image:1up6.jpg|left|200px]]
[[Image:1up6.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1up6 |SIZE=350|CAPTION= <scene name='initialview01'>1up6</scene>, resolution 2.55&Aring;
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The line below this paragraph, containing "STRUCTURE_1up6", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+G'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,3(4)-beta-glucanase Endo-1,3(4)-beta-glucanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.6 3.2.1.6] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1up6| PDB=1up6 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1up6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1up6 OCA], [http://www.ebi.ac.uk/pdbsum/1up6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1up6 RCSB]</span>
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}}
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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]
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[[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]]
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[[Category: family4 hydrolase]]
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[[Category: Family4 hydrolase]]
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[[Category: nad dependent]]
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[[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 Mar 31 00:13:27 2008''
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Revision as of 08:31, 3 May 2008

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


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

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