1cel: Difference between revisions

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[[Image:1cel.~~jpg~~|left|200px]]

[[Image:1cel.png|left|200px]]

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~~'''~~THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI~~'''~~

===THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8036495}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8036495 is the PubMed ID number.

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==About this Structure==

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[[Category: Divne, C.]]

[[Category: Jones, T A.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:38:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:38:28 2008''

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-[[Image:1cel.jpg|left|200px]]
+{{Seed}}
+[[Image:1cel.png|left|200px]]
 <!--
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 {{STRUCTURE_1cel|  PDB=1cel  |  SCENE=  }}
-'''THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI'''
+===THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8036495}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8036495 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8036495}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Divne, C.]]
 [[Category: Jones, T A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:38:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:38:28 2008''