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1azh

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Revision as of 07:58, 10 September 2015

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

Structural highlights

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

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

Three-dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel beta-sheet structure of the CBD fold was preserved in all engineered peptides. The three-dimensional NMR-based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N-terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.,Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T Protein Sci. 1997 Feb;6(2):294-303. PMID:9041630^[1]

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

References

↑ Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T. Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei. Protein Sci. 1997 Feb;6(2):294-303. PMID:9041630

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Atcc 13631 | Mattinen, M L | Cellulase | Nuclear magnetic resonance spectroscopy | Protein-carbohydrate interaction

@@ Line 2: / Line 2: @@
 <StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1azh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AZH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1azh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AZH FirstGlance]. <br>
-</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 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] </span></td></tr>
+</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=1azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [http://www.ebi.ac.uk/pdbsum/1azh 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=1azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azh OCA], [http://pdbe.org/1azh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [http://www.ebi.ac.uk/pdbsum/1azh PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GUX1_TRIRE GUX1_TRIRE]] 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.
+[[http://www.uniprot.org/uniprot/GUX1_HYPJE 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Cellulose 1,4-beta-cellobiosidase]]
+[[Category: Atcc 13631]]
-[[Category: Trichoderma reesei]]
 [[Category: Mattinen, M L]]
 [[Category: Cellulase]]
 [[Category: Nuclear magnetic resonance spectroscopy]]
 [[Category: Protein-carbohydrate interaction]]

1azh

From Proteopedia

Revision as of 07:58, 10 September 2015

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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