4cg3 - Revision history

OCA at 12:09, 20 December 2023

OCA — Wed, 20 Dec 2023 12:09:50 GMT

←Older revision		Revision as of 12:09, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.55Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [https://pdbe.org/4cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [https://pdbe.org/4cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU]] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>	+	[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.
		+
		+	Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca.,Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714<ref>PMID:24728714</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4cg3" style="background-color:#fffaf0;"></div>

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

OCA at 17:44, 7 September 2022

OCA — Wed, 07 Sep 2022 17:44:35 GMT

←Older revision		Revision as of 17:44, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cg3' size='340' side='right'caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4cg3' size='340' side='right'caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"thermonospora_fusca"_henssen_1957 "thermonospora~~ fusca~~" henssen 1957~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [https://pdbe.org/4cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [~~http~~://pdbe.org/4cg3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU]] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
-	~~Bacterial cutinases are promising catalysts for~~ the ~~modification and degradation~~ of the ~~widely used plastic polyethylene terephthalate~~ (~~PET~~). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (~~TfCut2) in free as well as in inhibitor~~-~~bound form~~. ~~Together with our analysis of the thermal stability and modelling studies~~, ~~we suggest possible reasons for the outstanding thermostability in comparison to~~ the ~~less thermostable homolog from Thermobifida alba AHK119~~ and ~~propose~~ a ~~model~~ for ~~the binding of the enzyme towards its polymeric substrate~~. ~~The TfCut2 structure is~~ the ~~basis for the rational design~~ of ~~catalytically more efficient enzyme variants for~~ the ~~hydrolysis of~~ PET ~~and other synthetic polyesters.~~	+
-		+
-	~~Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca~~.,~~Roth C~~, ~~Wei R~~, ~~Oeser T, Then J~~, ~~Follner C, Zimmermann W, Strater N Appl Microbiol Biotechnol~~. ~~2014 Apr 13~~. PMID:~~24728714~~<ref>PMID:24728714</ref>	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U.S. National Library of Medicine.~~<br>	+
-	</~~div~~>	+
-	<~~div class="pdbe-citations 4cg3" style="background-color~~:~~#fffaf0;"~~></~~div~~>	+

	==See Also==		==See Also==
Line 25:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Thermonospora fusca henssen 1957]]
-	[[Category: Cutinase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Foellner, C]]	+	[[Category: Thermobifida fusca]]
-	[[Category: Oeser, T]]	+	[[Category: Foellner C]]
-	[[Category: Roth, C]]	+	[[Category: Oeser T]]
-	[[Category: Straeter, N]]	+	[[Category: Roth C]]
-	[[Category: Then, J]]	+	[[Category: Straeter N]]
-	[[Category: Wei, R]]	+	[[Category: Then J]]
-	[[Category: Zimmermann, W]]	+	[[Category: Wei R]]
-	~~[[Category: Alpha-beta- fold]]~~	+	[[Category: Zimmermann W]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Pet degradation~~]]	+

OCA at 16:25, 28 August 2019

OCA — Wed, 28 Aug 2019 16:25:40 GMT

←Older revision		Revision as of 16:25, 28 August 2019
Line 1:		Line 1:
-	~~{{Large structure}}~~	+
	==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==		==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==
-	<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='4cg3' size='340' side='right'caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://pdbe.org/4cg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://pdbe.org/4cg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
	</table>		</table>
-	{{Large structure}}
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:

	==See Also==		==See Also==
-	*[[Cutinase\|Cutinase]]	+	*[[Cutinase 3D structures\|Cutinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 27:
	[[Category: Thermonospora fusca henssen 1957]]		[[Category: Thermonospora fusca henssen 1957]]
	[[Category: Cutinase]]		[[Category: Cutinase]]
		+	[[Category: Large Structures]]
	[[Category: Foellner, C]]		[[Category: Foellner, C]]
	[[Category: Oeser, T]]		[[Category: Oeser, T]]

OCA at 07:47, 16 November 2017

OCA — Thu, 16 Nov 2017 07:47:43 GMT

←Older revision		Revision as of 07:47, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Thermonospora fusca henssen 1957]]
	[[Category: Cutinase]]		[[Category: Cutinase]]
	[[Category: Foellner, C]]		[[Category: Foellner, C]]

OCA at 18:51, 11 August 2016

OCA — Thu, 11 Aug 2016 18:51:47 GMT

←Older revision		Revision as of 18:51, 11 August 2016
Line 1:		Line 1:
		+	{{Large structure}}
	==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==		==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==
	<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://pdbe.org/4cg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cg3 ProSAT]</span></td></tr>
	</table>		</table>
		+	{{Large structure}}
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 18:
	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 4cg3" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cutinase\|Cutinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:05, 20 January 2015

OCA — Tue, 20 Jan 2015 09:05:04 GMT

←Older revision		Revision as of 09:05, 20 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum]</span></td></tr>
-	<table>	+	</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Cutinase]]		[[Category: Cutinase]]
-	[[Category: Foellner, C.]]	+	[[Category: Foellner, C]]
-	[[Category: Oeser, T.]]	+	[[Category: Oeser, T]]
-	[[Category: Roth, C.]]	+	[[Category: Roth, C]]
-	[[Category: Straeter, N.]]	+	[[Category: Straeter, N]]
-	[[Category: Then, J.]]	+	[[Category: Then, J]]
-	[[Category: Wei, R.]]	+	[[Category: Wei, R]]
-	[[Category: Zimmermann, W.]]	+	[[Category: Zimmermann, W]]
	[[Category: Alpha-beta- fold]]		[[Category: Alpha-beta- fold]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Pet degradation]]		[[Category: Pet degradation]]

OCA at 06:21, 25 June 2014

OCA — Wed, 25 Jun 2014 06:21:01 GMT

←Older revision		Revision as of 06:21, 25 June 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca==
		+	<StructureSection load='4cg3' size='340' side='right' caption='[[4cg3]], [[Resolution\|resolution]] 1.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4cg3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CG3 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cg1\|4cg1]], [[4cg2\|4cg2]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cutinase Cutinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.74 3.1.1.74] </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=4cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cg3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cg3 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.

-	~~The entry 4cg3 is ON HOLD until Paper Publication~~	+	Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca.,Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714<ref>PMID:24728714</ref>

-	~~Authors: Roth~~, C.~~, Wei, R~~., Oeser, T., Then, J., ~~Foellner, C~~., Zimmermann, W.~~, Straeter, N.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Cutinase]]
		+	[[Category: Foellner, C.]]
		+	[[Category: Oeser, T.]]
		+	[[Category: Roth, C.]]
		+	[[Category: Straeter, N.]]
		+	[[Category: Then, J.]]
		+	[[Category: Wei, R.]]
		+	[[Category: Zimmermann, W.]]
		+	[[Category: Alpha-beta- fold]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pet degradation]]

OCA at 09:07, 25 December 2013

OCA — Wed, 25 Dec 2013 09:07:21 GMT

←Older revision		Revision as of 09:07, 25 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4cg3 is ON HOLD	+	The entry 4cg3 is ON HOLD until Paper Publication

	Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N.		Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N.

	Description: Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca		Description: Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca

OCA: Protected "4cg3" [edit=sysop:move=sysop]

OCA — Wed, 11 Dec 2013 12:47:04 GMT

Protected "4cg3" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:47, 11 December 2013

OCA: New page: '''Unreleased structure''' The entry 4cg3 is ON HOLD Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N. Description: Structural and functional ...

OCA — Wed, 11 Dec 2013 12:47:03 GMT

New page: '''Unreleased structure''' The entry 4cg3 is ON HOLD Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N. Description: Structural and functional ...

New page

'''Unreleased structure'''

The entry 4cg3 is ON HOLD

Authors: Roth, C., Wei, R., Oeser, T., Then, J., Foellner, C., Zimmermann, W., Straeter, N.

Description: Structural and functional studies on a thermostable polyethylene therephtalate degrading hydrolase from Thermobifida fusca