2his
From Proteopedia
(New page: 200px<br /> <applet load="2his" size="450" color="white" frame="true" align="right" spinBox="true" caption="2his, resolution 1.84Å" /> '''CELLULOMONAS FIMI X...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2HIS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HIS OCA]]. | + | 2HIS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. Active as [[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]]. Structure known Active Site: NUC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HIS OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9731776 9731776] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9731776 9731776] | ||
[[Category: Cellulomonas fimi]] | [[Category: Cellulomonas fimi]] | ||
| + | [[Category: Cellulose 1,4-beta-cellobiosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Birsan, C.]] | [[Category: Birsan, C.]] | ||
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[[Category: xylanase/cellulase]] | [[Category: xylanase/cellulase]] | ||
| - | ''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 11:31:01 2007'' |
Revision as of 09:26, 30 October 2007
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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]. Active as [Cellulose 1,4-beta-cellobiosidase], with EC number [3.2.1.91]. Structure known Active Site: NUC. 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
Page seeded by OCA on Tue Oct 30 11:31:01 2007
