1exp: Difference between revisions
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|PDB= 1exp |SIZE=350|CAPTION= <scene name='initialview01'>1exp</scene>, resolution 1.8Å | |PDB= 1exp |SIZE=350|CAPTION= <scene name='initialview01'>1exp</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=ABC:Acid+Base+Catalyst'>ABC</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+The+Fluoroce+...'>NUC</scene> | |SITE= <scene name='pdbsite=ABC:Acid+Base+Catalyst'>ABC</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+The+Fluoroce+...'>NUC</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=G2F:2-DEOXY-2FLUORO-GLUCOSE'>G2F</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1exp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exp OCA], [http://www.ebi.ac.uk/pdbsum/1exp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1exp RCSB]</span> | |||
}} | }} | ||
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[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:41 2008'' | ||
Revision as of 17:11, 30 March 2008
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| 1exp, resolution 1.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | ABC and NUC | ||||||||||||
| Ligands: | G2F, GLC | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
BETA-1,4-GLYCANASE CEX-CD
Overview
The three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by 19F-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme's specificity.
About this Structure
1EXP is a Single protein structure of sequence from Cellulomonas fimi. Full crystallographic information is available from OCA.
Reference
Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase., White A, Tull D, Johns K, Withers SG, Rose DR, Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541
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