2bog
From Proteopedia
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|PDB= 2bog |SIZE=350|CAPTION= <scene name='initialview01'>2bog</scene>, resolution 1.04Å | |PDB= 2bog |SIZE=350|CAPTION= <scene name='initialview01'>2bog</scene>, resolution 1.04Å | ||
|SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+X'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+X'>AC1</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bog OCA], [http://www.ebi.ac.uk/pdbsum/2bog PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bog RCSB]</span> | ||
}} | }} | ||
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[[Category: tim a/b fold]] | [[Category: tim a/b fold]] | ||
| - | ''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 02:09:22 2008'' |
Revision as of 23:09, 30 March 2008
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| , resolution 1.04Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE
Overview
Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.
About this Structure
2BOG is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.
Reference
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion., Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA, Biochemistry. 2005 Oct 4;44(39):12915-22. PMID:16185060
Page seeded by OCA on Mon Mar 31 02:09:22 2008
