4i5u - Revision history

OCA at 08:43, 9 November 2022

2022-11-09T08:43:18Z

←Older revision		Revision as of 08:43, 9 November 2022
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	==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==		==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
-	<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution\|resolution]] 1.22Å' scene=''>	+	<StructureSection load='4i5u' size='340' side='right'caption='[[4i5u]], [[Resolution\|resolution]] 1.22Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4i5u]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_16454 Atcc 16454~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4I5U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4i5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum], [https://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens] and [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I5U FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4i5r\|4i5r]]</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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [https://pdbe.org/4i5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [https://www.ebi.ac.uk/pdbsum/4i5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i5u ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [~~http~~://pdbe.org/4i5u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4i5u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4i5u ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:9882628</ref>	+	[https://www.uniprot.org/uniprot/Q5G2D4_9PEZI Q5G2D4_9PEZI] [https://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:9882628</ref> [https://www.uniprot.org/uniprot/GUX2_HYPJE GUX2_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 ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 16454~~]]	+	[[Category: Chaetomium thermophilum]]
-	[[Category: ~~Arnold, F H~~]]	+	[[Category: Humicola insolens]]
-	[[Category: ~~Wu, I~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Cellobiohydrolase~~]]	+	[[Category: Trichoderma reesei]]
-	[[Category: ~~Chimera protein~~]]	+	[[Category: Arnold FH]]
-	[[Category: ~~Glycoside hydrolase]]~~	+	[[Category: Wu I]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 21:23, 5 August 2016

2016-08-05T21:23:22Z

←Older revision		Revision as of 21:23, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==		==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
	<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution\|resolution]] 1.22Å' scene=''>		<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution\|resolution]] 1.22Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u 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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://pdbe.org/4i5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i5u ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:9882628</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 17:		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 4i5u" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:29, 21 December 2014

2014-12-21T12:29:16Z

←Older revision		Revision as of 12:29, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4i5u\| PDB=4i5u \| SCENE= }}~~	+	==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
-	===Crystal structure of a fungal chimeric cellobiohydrolase Cel6A===	+	<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution\|resolution]] 1.22Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23404363}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4i5u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I5U FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4i5r\|4i5r]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Thermostability is an important feature in industrial enzymes: it increases biocatalyst lifetime and enables reactions at higher temperatures, where faster rates and other advantages ultimately reduce the cost of biocatalysis. Here we report the thermostabilization of a chimeric fungal family 6 cellobiohydrolase (HJPlus) by directed evolution using random mutagenesis and recombination of beneficial mutations. Thermostable variant 3C6P has a half-life of 280 min at 75 degrees C and a T50 of 80.1 degrees C, a approximately 15 degrees C increase over the thermostable Cel6A from Humicola insolens (HiCel6A) and a approximately 20 degrees C increase over that from Hypocrea jecorina (HjCel6A). Most of the mutations also stabilize the less-stable HjCel6A, the wild-type Cel6A closest in sequence to 3C6P. During a 60-h Avicel hydrolysis, 3C6P released 2.4 times more cellobiose equivalents at its optimum temperature (Topt ) of 75 degrees C than HiCel6A at its Topt of 60 degrees C. The total cellobiose equivalents released by HiCel6A at 60 degrees C after 60 h is equivalent to the total released by 3C6P at 75 degrees C after approximately 6 h, a 10-fold reduction in hydrolysis time. A binary mixture of thermostable Cel6A and Cel7A hydrolyzes Avicel synergistically and released 1.8 times more cellobiose equivalents than the wild-type mixture, both mixtures assessed at their respective Topt . Crystal structures of HJPlus and 3C6P, determined at 1.5 and 1.2 A resolution, indicate that the stabilization comes from improved hydrophobic interactions and restricted loop conformations by introduced proline residues. Biotechnol. Bioeng. (c) 2013 Wiley Periodicals, Inc.

-	~~==Function==~~	+	Engineered thermostable fungal Cel6A and Cel7A cellobiohydrolases hydrolyze cellulose efficiently at elevated temperatures.,Wu I, Arnold FH Biotechnol Bioeng. 2013 Feb 12. doi: 10.1002/bit.24864. PMID:23404363<ref>PMID:23404363</ref>
-	~~[[http~~:/~~/www~~.~~uniprot~~.~~org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:~~9882628~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4i5u]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4I5U OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023404363</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Arnold, F H.]]	+	</StructureSection>
-	[[Category: Wu, I.]]	+	[[Category: Atcc 16454]]
		+	[[Category: Arnold, F H]]
		+	[[Category: Wu, I]]
	[[Category: Cellobiohydrolase]]		[[Category: Cellobiohydrolase]]
	[[Category: Chimera protein]]		[[Category: Chimera protein]]
	[[Category: Glycoside hydrolase]]		[[Category: Glycoside hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 21:09, 19 June 2013

2013-06-19T21:09:55Z

←Older revision		Revision as of 21:09, 19 June 2013
Line 10:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023404363</ref><references group="xtra"/><references/>
	[[Category: Arnold, F H.]]		[[Category: Arnold, F H.]]
	[[Category: Wu, I.]]		[[Category: Wu, I.]]

OCA at 01:30, 4 April 2013

2013-04-04T01:30:21Z

←Older revision		Revision as of 01:30, 4 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4i5u\| PDB=4i5u \| SCENE= }}
		+	===Crystal structure of a fungal chimeric cellobiohydrolase Cel6A===
		+	{{ABSTRACT_PUBMED_23404363}}

-	The ~~entry 4i5u is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. 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.<ref>PMID:9882628</ref>

-	~~Authors~~: ~~Arnold, F~~.H.~~, Wu, I~~.	+	==About this Structure==
		+	[[4i5u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA].

-	~~Description~~: ~~Crystal structure of a fungal chimeric cellobiohydrolase Cel6A~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Arnold, F H.]]
		+	[[Category: Wu, I.]]
		+	[[Category: Cellobiohydrolase]]
		+	[[Category: Chimera protein]]
		+	[[Category: Glycoside hydrolase]]
		+	[[Category: Hydrolase]]

OCA at 20:48, 12 December 2012

2012-12-12T20:48:17Z

←Older revision		Revision as of 20:48, 12 December 2012
Line 3:		Line 3:
	The entry 4i5u is ON HOLD		The entry 4i5u is ON HOLD

-	Authors: Arnold, FH, Wu, I	+	Authors: Arnold, F.H., Wu, I.

	Description: Crystal structure of a fungal chimeric cellobiohydrolase Cel6A		Description: Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

OCA: Protected "4i5u" [edit=sysop:move=sysop]

2012-12-05T10:35:28Z

Protected "4i5u" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:35, 5 December 2012

OCA: New page: '''Unreleased structure''' The entry 4i5u is ON HOLD Authors: Arnold, FH, Wu, I Description: Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

2012-12-05T10:35:27Z

New page: '''Unreleased structure''' The entry 4i5u is ON HOLD Authors: Arnold, FH, Wu, I Description: Crystal structure of a fungal chimeric cellobiohydrolase Cel6A

New page

'''Unreleased structure'''

The entry 4i5u is ON HOLD

Authors: Arnold, FH, Wu, I

Description: Crystal structure of a fungal chimeric cellobiohydrolase Cel6A