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1exp
From Proteopedia
(New page: 200px<br /> <applet load="1exp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exp, resolution 1.8Å" /> '''BETA-1,4-GLYCANASE C...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1EXP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]]. | + | 1EXP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. Structure known Active Sites: ABC and NUC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:47:48 2007'' |
Revision as of 10:43, 30 October 2007
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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]. Structure known Active Sites: ABC and NUC. 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 Tue Oct 30 12:47:48 2007
