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1cel

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Revision as of 06:28, 29 November 2017

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

Structural highlights

1cel is a 2 chain structure with sequence from Atcc 13631. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Activity:	Cellulose 1,4-beta-cellobiosidase (non-reducing end), with EC number 3.2.1.91
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GUX1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science. 1994 Jul 22;265(5171):524-8. PMID:8036495

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cel"

Categories: Atcc 13631 | Divne, C | Jones, T A

@@ Line 1: / Line 1: @@
 ==THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI==
 <StructureSection load='1cel' size='340' side='right' caption='[[1cel]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cel OCA], [http://pdbe.org/1cel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cel RCSB], [http://www.ebi.ac.uk/pdbsum/1cel PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cel OCA], [http://pdbe.org/1cel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cel RCSB], [http://www.ebi.ac.uk/pdbsum/1cel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cel ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1cel" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cellobiohydrolase|Cellobiohydrolase]]
 == References ==
 <references/>

1cel

From Proteopedia

Revision as of 06:28, 29 November 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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