4c4d - Revision history

OCA at 12:03, 20 December 2023

OCA — Wed, 20 Dec 2023 12:03:19 GMT

←Older revision		Revision as of 12:03, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4D FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.32Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene></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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [https://pdbe.org/4c4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [https://www.ebi.ac.uk/pdbsum/4c4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4d 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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [https://pdbe.org/4c4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [https://www.ebi.ac.uk/pdbsum/4c4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4d 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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glycoside hydrolases (GHs) cleave glycosidic linkages in carbohydrates, typically via inverting or retaining mechanisms, the latter of which proceeds via a two-step mechanism that includes formation of a glycosyl-enzyme intermediate. We present two new structures of the catalytic domain of Hypocrea jecorina GH Family 7 cellobiohydrolase Cel7A, namely a Michaelis complex with a full cellononaose ligand and a glycosyl-enzyme intermediate, that reveal details of the 'static' reaction coordinate. We also employ transition path sampling to determine the 'dynamic' reaction coordinate for the catalytic cycle. The glycosylation reaction coordinate contains components of forming and breaking bonds and a conformational change in the nucleophile. Deglycosylation proceeds via a product-assisted mechanism wherein the glycosylation product, cellobiose, positions a water molecule for nucleophilic attack on the anomeric carbon of the glycosyl-enzyme intermediate. In concert with previous structures, the present results reveal the complete hydrolytic reaction coordinate for this naturally and industrially important enzyme family.
		+
		+	The Mechanism of Cellulose Hydrolysis by a Two-Step, Retaining Cellobiohydrolase Elucidated by Structural and Transition Path Sampling Studies.,Knott BC, Haddad Momeni M, Crowley MF, Mackenzie LF, Gotz AW, Sandgren M, Withers SG, Stahlberg J, Beckham GT J Am Chem Soc. 2013 Dec 16. PMID:24341799<ref>PMID:24341799</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c4d" 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>

OCA at 17:25, 7 September 2022

OCA — Wed, 07 Sep 2022 17:25:37 GMT

←Older revision		Revision as of 17:25, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c4d' size='340' side='right'caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>		<StructureSection load='4c4d' size='340' side='right'caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_13631 Atcc 13631~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C4D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=~~PEG~~:~~DI(HYDROXYETHYL)ETHER~~'>~~PEG~~</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene></td></tr>
-	~~<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [https://pdbe.org/4c4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [https://www.ebi.ac.uk/pdbsum/4c4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4d ProSAT]</span></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [~~http~~://pdbe.org/4c4d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c4d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4d 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.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Glycoside hydrolases (GHs) cleave glycosidic linkages in carbohydrates, typically via inverting or retaining mechanisms, the latter of which proceeds via a two-step mechanism that includes formation of a glycosyl-enzyme intermediate. We present two new structures of the catalytic domain of Hypocrea jecorina GH Family 7 cellobiohydrolase Cel7A, namely a Michaelis complex with a full cellononaose ligand and a glycosyl-enzyme intermediate, that reveal details of the 'static' reaction coordinate. We also employ transition path sampling to determine the 'dynamic' reaction coordinate for the catalytic cycle. The glycosylation reaction coordinate contains components of forming and breaking bonds and a conformational change in the nucleophile. Deglycosylation proceeds via a product-assisted mechanism wherein the glycosylation product, cellobiose, positions a water molecule for nucleophilic attack on the anomeric carbon of the glycosyl-enzyme intermediate. In concert with previous structures, the present results reveal the complete hydrolytic reaction coordinate for this naturally and industrially important enzyme family.	+
-		+
-	The Mechanism of Cellulose Hydrolysis by a Two-Step, Retaining Cellobiohydrolase Elucidated by Structural and Transition Path Sampling Studies.,Knott BC, Haddad Momeni M, Crowley MF, Mackenzie LF, Gotz AW, Sandgren M, Withers SG, Stahlberg J, Beckham GT J Am Chem Soc. 2013 Dec 16. PMID:24341799<ref>PMID:24341799</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c4d" 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: Haddad-Momeni, M]]	+	[[Category: Trichoderma reesei]]
-	[[Category: Mackenzie, L]]	+	[[Category: Haddad-Momeni M]]
-	[[Category: Sandgren, M]]	+	[[Category: Mackenzie L]]
-	[[Category: Stahlberg, J]]	+	[[Category: Sandgren M]]
-	[[Category: Withers~~, S G]]~~	+	[[Category: Stahlberg J]]
-	~~[[Category: Cellobiohydrolase]]~~	+	[[Category: Withers SG]]
-	~~[[Category: Cellulase]]~~	+
-	~~[[Category: Glycoside hydrolase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:42, 11 March 2020

OCA — Wed, 11 Mar 2020 07:42:17 GMT

←Older revision		Revision as of 07:42, 11 March 2020
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Cellobiohydrolase\|Cellobiohydrolase]]	+	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:26, 20 March 2019

OCA — Wed, 20 Mar 2019 09:26:09 GMT

←Older revision		Revision as of 09:26, 20 March 2019
Line 1:		Line 1:

	==Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside==		==Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside==
-	<StructureSection load='4c4d' size='340' side='right' caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>	+	<StructureSection load='4c4d' size='340' side='right'caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4D FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL~~-D-~~GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=~~PEG~~:~~DI(HYDROXYETHYL)ETHER~~'>~~PEG~~</scene>, <scene name='pdbligand=~~G2F~~:~~2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE~~'>~~G2F~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<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='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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</td></tr>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4c4d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4c4d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cellobiohydrolase\|Cellobiohydrolase]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 13631]]		[[Category: Atcc 13631]]
		+	[[Category: Large Structures]]
	[[Category: Haddad-Momeni, M]]		[[Category: Haddad-Momeni, M]]
	[[Category: Mackenzie, L]]		[[Category: Mackenzie, L]]

OCA at 18:54, 5 August 2016

OCA — Fri, 05 Aug 2016 18:54:31 GMT

←Older revision		Revision as of 18:54, 5 August 2016
Line 1:		Line 1:
		+
	==Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside==		==Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside==
	<StructureSection load='4c4d' size='340' side='right' caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>		<StructureSection load='4c4d' size='340' side='right' caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</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='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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [http://www.ebi.ac.uk/pdbsum/4c4d 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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [http://pdbe.org/4c4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [http://www.ebi.ac.uk/pdbsum/4c4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4c4d" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:59, 25 December 2014

OCA — Thu, 25 Dec 2014 04:59:43 GMT

←Older revision		Revision as of 04:59, 25 December 2014
Line 9:		Line 9:
	<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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [http://www.ebi.ac.uk/pdbsum/4c4d 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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [http://www.ebi.ac.uk/pdbsum/4c4d PDBsum]</span></td></tr>
	</table>		</table>
		+	== 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:04, 21 December 2014

OCA — Sun, 21 Dec 2014 17:04:35 GMT

←Older revision		Revision as of 17:04, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c4d\| PDB=4c4d \| SCENE= }}~~	+	==Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside==
-	===Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside===	+	<StructureSection load='4c4d' size='340' side='right' caption='[[4c4d]], [[Resolution\|resolution]] 1.32Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24341799}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c4d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene></td></tr>
		+	<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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4c\|4c4c]]</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=4c4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4d RCSB], [http://www.ebi.ac.uk/pdbsum/4c4d PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glycoside hydrolases (GHs) cleave glycosidic linkages in carbohydrates, typically via inverting or retaining mechanisms, the latter of which proceeds via a two-step mechanism that includes formation of a glycosyl-enzyme intermediate. We present two new structures of the catalytic domain of Hypocrea jecorina GH Family 7 cellobiohydrolase Cel7A, namely a Michaelis complex with a full cellononaose ligand and a glycosyl-enzyme intermediate, that reveal details of the 'static' reaction coordinate. We also employ transition path sampling to determine the 'dynamic' reaction coordinate for the catalytic cycle. The glycosylation reaction coordinate contains components of forming and breaking bonds and a conformational change in the nucleophile. Deglycosylation proceeds via a product-assisted mechanism wherein the glycosylation product, cellobiose, positions a water molecule for nucleophilic attack on the anomeric carbon of the glycosyl-enzyme intermediate. In concert with previous structures, the present results reveal the complete hydrolytic reaction coordinate for this naturally and industrially important enzyme family.

-	~~==Function==~~	+	The Mechanism of Cellulose Hydrolysis by a Two-Step, Retaining Cellobiohydrolase Elucidated by Structural and Transition Path Sampling Studies.,Knott BC, Haddad Momeni M, Crowley MF, Mackenzie LF, Gotz AW, Sandgren M, Withers SG, Stahlberg J, Beckham GT J Am Chem Soc. 2013 Dec 16. PMID:24341799<ref>PMID:24341799</ref>
-	~~[[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~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4c4d]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4C4D OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024341799</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Haddad-Momeni, M.]]	+	</StructureSection>
-	[[Category: Mackenzie, L.]]	+	[[Category: Atcc 13631]]
-	[[Category: Sandgren, M.]]	+	[[Category: Haddad-Momeni, M]]
-	[[Category: Stahlberg, J.]]	+	[[Category: Mackenzie, L]]
-	[[Category: Withers, S G.]]	+	[[Category: Sandgren, M]]
		+	[[Category: Stahlberg, J]]
		+	[[Category: Withers, S G]]
	[[Category: Cellobiohydrolase]]		[[Category: Cellobiohydrolase]]
-	[[Category: Cellulase.]]	+	[[Category: Cellulase]]
	[[Category: Glycoside hydrolase]]		[[Category: Glycoside hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 10:32, 8 January 2014

OCA — Wed, 08 Jan 2014 10:32:03 GMT

←Older revision		Revision as of 10:32, 8 January 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c4d\| PDB=4c4d \| SCENE= }}
		+	===Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside===
		+	{{ABSTRACT_PUBMED_24341799}}

-	The ~~entry 4c4d is ON HOLD until Paper Publication~~	+	==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.

-	~~Authors~~: ~~Haddad-Momeni, M~~.~~, Mackenzie, L~~.~~, Sandgren, M~~.~~, Withers, S.G., Stahlberg, J~~.	+	==About this Structure==
		+	[[4c4d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4D OCA].

-	~~Description~~: ~~Covalent glycosyl~~-~~enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside~~	+	==Reference==
		+	<ref group="xtra">PMID:024341799</ref><references group="xtra"/><references/>
		+	[[Category: Haddad-Momeni, M.]]
		+	[[Category: Mackenzie, L.]]
		+	[[Category: Sandgren, M.]]
		+	[[Category: Stahlberg, J.]]
		+	[[Category: Withers, S G.]]
		+	[[Category: Cellobiohydrolase]]
		+	[[Category: Cellulase.]]
		+	[[Category: Glycoside hydrolase]]
		+	[[Category: Hydrolase]]

OCA at 03:17, 20 September 2013

OCA — Fri, 20 Sep 2013 03:17:35 GMT

←Older revision		Revision as of 03:17, 20 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c4d is ON HOLD	+	The entry 4c4d is ON HOLD until Paper Publication

	Authors: Haddad-Momeni, M., Mackenzie, L., Sandgren, M., Withers, S.G., Stahlberg, J.		Authors: Haddad-Momeni, M., Mackenzie, L., Sandgren, M., Withers, S.G., Stahlberg, J.

-	Description: Hypocrea jecorina ~~Cel7A~~ E217Q mutant ~~with cellonanoase bound in the active site~~	+	Description: Covalent glycosyl-enzyme intermediate of Hypocrea jecorina Cel7a E217Q mutant trapped using DNP-2-deoxy-2-fluoro-cellotrioside

OCA: Protected "4c4d" [edit=sysop:move=sysop]

OCA — Thu, 12 Sep 2013 04:30:59 GMT

Protected "4c4d" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:30, 12 September 2013