1exp: Difference between revisions
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[[Image:1exp.gif|left|200px]] | [[Image:1exp.gif|left|200px]] | ||
'''BETA-1,4-GLYCANASE CEX-CD''' | {{Structure | ||
|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> | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''BETA-1,4-GLYCANASE CEX-CD''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EXP is a [ | 1EXP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8564541 8564541] | ||
[[Category: Cellulomonas fimi]] | [[Category: Cellulomonas fimi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:44 2008'' | ||
Revision as of 09:01, 20 March 2008
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| 1exp, resolution 1.8Å | |||||||||||||
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| Sites: | ABC and NUC | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 11:01:44 2008
