1up6
From Proteopedia
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|PDB= 1up6 |SIZE=350|CAPTION= <scene name='initialview01'>1up6</scene>, resolution 2.55Å | |PDB= 1up6 |SIZE=350|CAPTION= <scene name='initialview01'>1up6</scene>, resolution 2.55Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+G'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+G'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Withers, S G.]] | [[Category: Withers, S G.]] | ||
[[Category: Yip, V L.]] | [[Category: Yip, V L.]] | ||
| - | [[Category: G6P]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: SO4]] | ||
[[Category: 6-phospho-beta-glucosidase]] | [[Category: 6-phospho-beta-glucosidase]] | ||
[[Category: family4 hydrolase]] | [[Category: family4 hydrolase]] | ||
[[Category: nad dependent]] | [[Category: nad dependent]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:13:27 2008'' |
Revision as of 21:13, 30 March 2008
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| , resolution 2.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Endo-1,3(4)-beta-glucanase, with EC number 3.2.1.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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