1lf1
From Proteopedia
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| - | [[Image:1lf1.gif|left|200px]] | + | [[Image:1lf1.gif|left|200px]] |
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| - | '''Crystal Structure of Cel5 from Alkalophilic Bacillus sp.''' | + | {{Structure |
| + | |PDB= 1lf1 |SIZE=350|CAPTION= <scene name='initialview01'>1lf1</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Cel5 from Alkalophilic Bacillus sp.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LF1 is a [ | + | 1LF1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LF1 OCA]. |
==Reference== | ==Reference== | ||
| - | A novel combination of two classic catalytic schemes., Shaw A, Bott R, Vonrhein C, Bricogne G, Power S, Day AG, J Mol Biol. 2002 Jul 5;320(2):303-9. PMID:[http:// | + | A novel combination of two classic catalytic schemes., Shaw A, Bott R, Vonrhein C, Bricogne G, Power S, Day AG, J Mol Biol. 2002 Jul 5;320(2):303-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12079387 12079387] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
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[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
| - | ''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 12:30:09 2008'' |
Revision as of 10:30, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Cel5 from Alkalophilic Bacillus sp.
Overview
The crystal structure of an alkaline Bacillus cellulase catalytic core, from glucoside hydrolase family 5, reveals a novel combination of the catalytic machinery of two classic textbook enzymes. The enzyme has the expected two glutamate residues in close proximity to one another in the active-site that are typical of retaining cellulases. However, the proton donor, glutamate 139 is also unexpectedly a member of a serine-histidine-glutamate catalytic triad, forming a novel combination of catalytic machineries. Structure and sequence analysis of glucoside hydrolase family 5 reveal that the triad is highly conserved, but with variations at the equivalent of the serine position. We speculate that the purpose of this novel catalytic triad is to control the protonation of the acid/base glutamate, facilitating the first step of the catalytic reaction, protonation of the substrate, by the proton donor glutamate. If correct, this will be a novel use for a catalytic triad.
About this Structure
1LF1 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A novel combination of two classic catalytic schemes., Shaw A, Bott R, Vonrhein C, Bricogne G, Power S, Day AG, J Mol Biol. 2002 Jul 5;320(2):303-9. PMID:12079387
Page seeded by OCA on Thu Mar 20 12:30:09 2008
