1cel: Difference between revisions
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[[Image:1cel.jpg|left|200px]] | [[Image:1cel.jpg|left|200px]] | ||
'''THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI''' | {{Structure | ||
|PDB= 1cel |SIZE=350|CAPTION= <scene name='initialview01'>1cel</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=IBZ:2-IODOBENZYLTHIO GROUP'>IBZ</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CEL is a [ | 1CEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEL OCA]. | ||
==Reference== | ==Reference== | ||
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA, Science. 1994 Jul 22;265(5171):524-8. PMID:[http:// | The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA, Science. 1994 Jul 22;265(5171):524-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8036495 8036495] | ||
[[Category: Cellulose 1,4-beta-cellobiosidase]] | [[Category: Cellulose 1,4-beta-cellobiosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
''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 10:23:25 2008'' |
Revision as of 11:23, 20 March 2008
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, resolution 1.8Å | |||||||
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Ligands: | , , and | ||||||
Activity: | Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI
OverviewOverview
Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.
About this StructureAbout this Structure
1CEL is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA, Science. 1994 Jul 22;265(5171):524-8. PMID:8036495
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