1azh - Revision history

OCA at 15:29, 13 March 2024

OCA — Wed, 13 Mar 2024 15:29:50 GMT

←Older revision		Revision as of 15:29, 13 March 2024
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	==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==		==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==
-	<StructureSection load='1azh' size='340' side='right'caption='[[1azh~~]], [[NMR_Ensembles_of_Models \| 14 NMR models~~]]' scene=''>	+	<StructureSection load='1azh' size='340' side='right'caption='[[1azh]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1azh]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1AZH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1azh]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[https://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azh OCA], [https://pdbe.org/1azh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [https://www.ebi.ac.uk/pdbsum/1azh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azh ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azh OCA], [https://pdbe.org/1azh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [https://www.ebi.ac.uk/pdbsum/1azh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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.	+	[https://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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1azh ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1azh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== 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<ref>PMID:9041630</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]		*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 13631]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Mattinen, M L~~]]	+	[[Category: Trichoderma reesei]]
-	[[Category: ~~Cellulase]]~~	+	[[Category: Mattinen M-L]]
-	~~[[Category: Nuclear magnetic resonance spectroscopy]]~~	+
-	~~[[Category: Protein~~-~~carbohydrate interaction~~]]	+

OCA at 15:02, 2 June 2021

OCA — Wed, 02 Jun 2021 15:02:53 GMT

←Older revision		Revision as of 15:02, 2 June 2021
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	<StructureSection load='1azh' size='340' side='right'caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>		<StructureSection load='1azh' size='340' side='right'caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<table><tr><td colspan='2'>[[1azh]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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_(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>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [https://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~~://pdbe.org/1azh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1azh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1azh ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1azh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azh OCA], [https://pdbe.org/1azh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [https://www.ebi.ac.uk/pdbsum/1azh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~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.	+	[[https://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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:44, 28 August 2019

OCA — Wed, 28 Aug 2019 16:44:54 GMT

←Older revision		Revision as of 16:44, 28 August 2019
Line 1:		Line 1:

	==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==		==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==
-	<StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>	+	<StructureSection load='1azh' size='340' side='right'caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<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>		<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>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/1azh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/1azh_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 13631]]		[[Category: Atcc 13631]]
		+	[[Category: Large Structures]]
	[[Category: Mattinen, M L]]		[[Category: Mattinen, M L]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Nuclear magnetic resonance spectroscopy]]		[[Category: Nuclear magnetic resonance spectroscopy]]
	[[Category: Protein-carbohydrate interaction]]		[[Category: Protein-carbohydrate interaction]]

OCA at 11:10, 22 November 2017

OCA — Wed, 22 Nov 2017 11:10:23 GMT

←Older revision		Revision as of 11:10, 22 November 2017
Line 1:		Line 1:
		+
	==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==		==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==
	<StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>		<StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
Line 4:		Line 5:
	<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>		<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_(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>		</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://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>	+	<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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1azh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cellobiohydrolase\|Cellobiohydrolase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:41, 8 February 2016

OCA — Mon, 08 Feb 2016 04:41:56 GMT

←Older revision		Revision as of 04:41, 8 February 2016
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1azh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:58, 10 September 2015

OCA — Thu, 10 Sep 2015 07:58:09 GMT

←Older revision		Revision as of 07:58, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>		<StructureSection load='1azh' size='340' side='right' caption='[[1azh]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== 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>		</table>
	== Function ==		== 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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 26:		Line 26:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1azh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cellulose 1,4-beta-cellobiosidase]]~~	+	[[Category: Atcc 13631]]
-	~~[[Category: Trichoderma reesei~~]]	+
	[[Category: Mattinen, M L]]		[[Category: Mattinen, M L]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Nuclear magnetic resonance spectroscopy]]		[[Category: Nuclear magnetic resonance spectroscopy]]
	[[Category: Protein-carbohydrate interaction]]		[[Category: Protein-carbohydrate interaction]]

OCA at 20:42, 24 December 2014

OCA — Wed, 24 Dec 2014 20:42:15 GMT

←Older revision		Revision as of 20:42, 24 December 2014
Line 6:		Line 6:
	<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://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [http://www.ebi.ac.uk/pdbsum/1azh PDBsum]</span></td></tr>
	</table>		</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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:05, 22 December 2014

OCA — Mon, 22 Dec 2014 10:05:54 GMT

←Older revision		Revision as of 10:05, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== 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/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>
-	</td></tr><tr><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 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>
-	<tr><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://www.rcsb.org/pdb/explore.do?structureId=1azh RCSB], [http://www.ebi.ac.uk/pdbsum/1azh PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:
	[[Category: Cellulose 1,4-beta-cellobiosidase]]		[[Category: Cellulose 1,4-beta-cellobiosidase]]
	[[Category: Trichoderma reesei]]		[[Category: Trichoderma reesei]]
-	[[Category: Mattinen, M L.]]	+	[[Category: Mattinen, M L]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Nuclear magnetic resonance spectroscopy]]		[[Category: Nuclear magnetic resonance spectroscopy]]
	[[Category: Protein-carbohydrate interaction]]		[[Category: Protein-carbohydrate interaction]]

OCA at 03:13, 7 August 2014

OCA — Thu, 07 Aug 2014 03:13:36 GMT

←Older revision		Revision as of 03:13, 7 August 2014
Line 1:		Line 1:
-	[[~~Image~~:1azh.~~png\|left~~\|200px]]	+	==THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 14 STRUCTURES==
		+	<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>
		+	</td></tr><tr><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>
		+	<tr><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>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/1azh_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== 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.

-	~~{{STRUCTURE_1azh\| PDB=1azh \| SCENE= }}~~	+	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<ref>PMID:9041630</ref>

-	~~===THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI~~, ~~NMR, 14 STRUCTURES===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9041630}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[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].~~	+

	==See Also==		==See Also==
	*[[Cellobiohydrolase\|Cellobiohydrolase]]		*[[Cellobiohydrolase\|Cellobiohydrolase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009041630<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cellulose 1,4-beta-cellobiosidase]]		[[Category: Cellulose 1,4-beta-cellobiosidase]]
	[[Category: Trichoderma reesei]]		[[Category: Trichoderma reesei]]

OCA at 08:56, 20 October 2012

OCA — Sat, 20 Oct 2012 08:56:57 GMT

←Older revision		Revision as of 08:56, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1azh]] is a 1 chain structure ~~of [[Cellobiohydrolase]]~~ 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].	+	[[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].

	==See Also==		==See Also==