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2his

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[[Image:2his.gif|left|200px]]
[[Image:2his.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2his |SIZE=350|CAPTION= <scene name='initialview01'>2his</scene>, resolution 1.84&Aring;
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The line below this paragraph, containing "STRUCTURE_2his", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=NUC:Catalytic+Nucleophile,+Covalently+Linked+To+Cellobiose'>NUC</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2his| PDB=2his | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE'''
'''CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE'''
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[[Category: Warren, R A.J.]]
[[Category: Warren, R A.J.]]
[[Category: Wither, S G.]]
[[Category: Wither, S G.]]
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[[Category: a/b barrel]]
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[[Category: A/b barrel]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: o-glycosyl]]
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[[Category: O-glycosyl]]
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[[Category: xylanase/cellulase]]
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[[Category: Xylanase/cellulase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:20:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:30:59 2008''
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Revision as of 03:20, 4 May 2008

Image:2his.gif

Template:STRUCTURE 2his

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 Page seeded by OCA on Sun May 4 06:20:46 2008

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