2his
From Proteopedia
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|PDB= 2his |SIZE=350|CAPTION= <scene name='initialview01'>2his</scene>, resolution 1.84Å | |PDB= 2his |SIZE=350|CAPTION= <scene name='initialview01'>2his</scene>, resolution 1.84Å | ||
|SITE= <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+Cellobiose'>NUC</scene> | |SITE= <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+Cellobiose'>NUC</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2his FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2his OCA], [http://www.ebi.ac.uk/pdbsum/2his PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2his RCSB]</span> | ||
}} | }} | ||
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[[Category: xylanase/cellulase]] | [[Category: xylanase/cellulase]] | ||
| - | ''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 03:30:59 2008'' |
Revision as of 00:31, 31 March 2008
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| , resolution 1.84Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE
Overview
The catalytic mechanism of 'retaining' beta-glycosidases has been the subject of considerable interest and debate for many years. The visualization of a covalent glycosyl enzyme intermediate by X-ray crystallography was first accomplished with a saccharide substrate substituted with fluorine at its 2-position. The structure implicated major roles for residue His 205 and for the 2-hydroxyl position of the proximal saccharide in binding and catalysis. Here we have studied the kinetic behavior of various His 205 mutants. One of these mutants, a double mutant H205N/E127A, has been used to stabilize a covalent glycosyl-enzyme intermediate involving an unsubstituted sugar, permitting crystallographic analysis of the interactions between its 2-hydroxyl group and the enzyme.
About this Structure
2HIS is a Single protein structure of sequence from Cellulomonas fimi. Full crystallographic information is available from OCA.
Reference
Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants., Notenboom V, Birsan C, Nitz M, Rose DR, Warren RA, Withers SG, Nat Struct Biol. 1998 Sep;5(9):812-8. PMID:9731776
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