1cel: Difference between revisions

Revision as of 13:05, 21 February 2008

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] with , , and as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 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

Page seeded by OCA on Thu Feb 21 12:05:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1cel.jpg|left|200px]]<br /><applet load="1cel" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cel.jpg|left|200px]]<br /><applet load="1cel" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cel, resolution 1.8&Aring;" />
 '''THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI'''<br />
 ==Overview==
-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.
+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 Structure==
-CEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, GLC, CA and IBZ as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEL OCA].
+CEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=IBZ:'>IBZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEL OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Divne, C.]]
-[[Category: Jones, T.A.]]
+[[Category: Jones, T A.]]
 [[Category: CA]]
 [[Category: GLC]]
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 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:23:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:16 2008''