1tml - Revision history

OCA at 07:28, 30 October 2024

2024-10-30T07:28:42Z

← Older revision		Revision as of 07:28, 30 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/1tml_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/1tml_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 05:36, 5 June 2024

2024-06-05T05:36:10Z

← Older revision		Revision as of 05:36, 5 June 2024
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	</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=1tml 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=1tml ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			One way to improve the economic feasibility of biomass conversion is to enhance the catalytic efficiency of cellulases through protein engineering. This requires that high-resolution structures of cellulases be available. Here we present the structure of E2cd, the catalytic domain of the thermophilic endocellulase E2 from Thermomonospora fusca, as determined by X-ray crystallography. The structure was solved by multiple isomorphous replacement at 2.6-A resolution and has been refined at 1.8-A resolution to an R-value of 18.4% for all reflections between 10- and 1.8-A resolution. The fold of E2cd is based on an unusual parallel beta-barrel and is equivalent to the fold determined for the catalytic domain of cellobiohydrolase II, an exocellulase from Trichoderma reesei [Rouvinen et al. (1990) Science 249, 380-385]. The active site cleft of the enzyme, approximately 11 A deep and running the entire length of the molecule, is seen to be completely free for ligand binding in the crystal. A 2.2-A resolution analysis of crystals of E2cd complexed with cellobiose, an inhibitor, shows how cellobiose binds in the active site and interacts with several residues which line the cleft. Catalytic roles are suggested for three aspartic acid residues at the active site. A comparison of the E2cd and CBHIIcd structures reveals a large difference in their active site accessibilities and supports the hypothesis that the main difference between endo- and exocellulases is the degree to which their active sites are accessible to substrate.

			Crystal structure of the catalytic domain of a thermophilic endocellulase.,Spezio M, Wilson DB, Karplus PA Biochemistry. 1993 Sep 28;32(38):9906-16. PMID:8399160<ref>PMID:8399160</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 1tml" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Glucanase 3D structures\|Glucanase 3D structures]]		*[[Glucanase 3D structures\|Glucanase 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:42, 1 May 2024

2024-05-01T08:42:29Z

← Older revision		Revision as of 08:42, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [https://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=1TML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TML FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tml]] 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TML 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]] 1.8Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]~~ </~~span~~></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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [https://pdbe.org/1tml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [https://www.ebi.ac.uk/pdbsum/1tml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml 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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [https://pdbe.org/1tml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [https://www.ebi.ac.uk/pdbsum/1tml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/GUN2_THEFU GUN2_THEFU]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1tml 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=1tml ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	One way to improve the economic feasibility of biomass conversion is to enhance the catalytic efficiency of cellulases through protein engineering. This requires that high-resolution structures of cellulases be available. Here we present the structure of E2cd, the catalytic domain of the thermophilic endocellulase E2 from Thermomonospora fusca, as determined by X-ray crystallography. The structure was solved by multiple isomorphous replacement at 2.6-A resolution and has been refined at 1.8-A resolution to an R-value of 18.4% for all reflections between 10- and 1.8-A resolution. The fold of E2cd is based on an unusual parallel beta-barrel and is equivalent to the fold determined for the catalytic domain of cellobiohydrolase II, an exocellulase from Trichoderma reesei [Rouvinen et al. (1990) Science 249, 380-385]. The active site cleft of the enzyme, approximately 11 A deep and running the entire length of the molecule, is seen to be completely free for ligand binding in the crystal. A 2.2-A resolution analysis of crystals of E2cd complexed with cellobiose, an inhibitor, shows how cellobiose binds in the active site and interacts with several residues which line the cleft. Catalytic roles are suggested for three aspartic acid residues at the active site. A comparison of the E2cd and CBHIIcd structures reveals a large difference in their active site accessibilities and supports the hypothesis that the main difference between endo- and exocellulases is the degree to which their active sites are accessible to substrate.

	~~Crystal structure of the catalytic domain of a thermophilic endocellulase.,Spezio M, Wilson DB, Karplus PA Biochemistry. 1993 Sep 28;32(38):9906-16. PMID:8399160<ref>PMID:8399160</ref>~~

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1tml" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Glucanase 3D structures\|Glucanase 3D structures]]		*[[Glucanase 3D structures\|Glucanase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Thermonospora fusca henssen 1957]]~~
	~~[[Category: Cellulase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Karplus, P A~~]]		[[Category: Thermobifida fusca]]
	[[Category: ~~Spezio, M~~]]		[[Category: Karplus PA]]
	[[Category: ~~Wilson, D B~~]]		[[Category: Spezio M]]
	[[Category: ~~Beta-amylase]]~~		[[Category: Wilson DB]]
	~~[[Category: Catalytic domain]]~~
	~~[[Category: Endocellulase~~]]

OCA at 09:29, 29 September 2021

2021-09-29T09:29:34Z

← Older revision		Revision as of 09:29, 29 September 2021
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	<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tml]] 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1TML FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [https://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=1TML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TML 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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [~~http~~://pdbe.org/1tml PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1tml PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml 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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [https://pdbe.org/1tml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [https://www.ebi.ac.uk/pdbsum/1tml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 14:03, 25 December 2019

2019-12-25T14:03:09Z

← Older revision		Revision as of 14:03, 25 December 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==		==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==
	<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tml]] 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tml]] 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML FirstGlance]. <br>
Line 29:		Line 29:

	==See Also==		==See Also==
	*[[Glucanase\|Glucanase]]		*[[Glucanase 3D structures\|Glucanase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Thermonospora fusca henssen 1957]]		[[Category: Thermonospora fusca henssen 1957]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
			[[Category: Large Structures]]
	[[Category: Karplus, P A]]		[[Category: Karplus, P A]]
	[[Category: Spezio, M]]		[[Category: Spezio, M]]

OCA at 08:52, 21 March 2018

2018-03-21T08:52:59Z

← Older revision		Revision as of 08:52, 21 March 2018
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==		==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==
	<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
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	</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://pdbe.org/1tml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml 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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://pdbe.org/1tml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/1tml_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tm/1tml_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>

OCA at 07:26, 7 February 2016

2016-02-07T07:26:44Z

← Older revision		Revision as of 07:26, 7 February 2016
Line 15:		Line 15:
	<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=1tml ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:10, 9 September 2015

2015-09-09T23:10:35Z

← Older revision		Revision as of 23:10, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermobifida_fusca Thermobifida~~ fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tml]] 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML 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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml 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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://pdbe.org/1tml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 25:		Line 25:
	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 1tml" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Thermonospora fusca henssen 1957]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
	~~[[Category: Thermobifida fusca]]~~
	[[Category: Karplus, P A]]		[[Category: Karplus, P A]]
	[[Category: Spezio, M]]		[[Category: Spezio, M]]

OCA at 12:58, 6 January 2015

2015-01-06T12:58:30Z

← Older revision		Revision as of 12:58, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML FirstGlance]. <br>		<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML 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>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml 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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml 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 34:		Line 34:
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]
	[[Category: Karplus, P A.]]		[[Category: Karplus, P A]]
	[[Category: Spezio, M.]]		[[Category: Spezio, M]]
	[[Category: Wilson, D B.]]		[[Category: Wilson, D B]]
	[[Category: Beta-amylase]]		[[Category: Beta-amylase]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
	[[Category: Endocellulase]]		[[Category: Endocellulase]]

OCA at 21:15, 28 September 2014

2014-09-28T21:15:20Z

← Older revision		Revision as of 21:15, 28 September 2014
Line 1:		Line 1:
	[[Image:~~1tml~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==
			<StructureSection load='1tml' size='340' side='right' caption='[[1tml]], [[Resolution\|resolution]] 1.80Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1tml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TML 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>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [http://www.ebi.ac.uk/pdbsum/1tml 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/tm/1tml_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 ==
			One way to improve the economic feasibility of biomass conversion is to enhance the catalytic efficiency of cellulases through protein engineering. This requires that high-resolution structures of cellulases be available. Here we present the structure of E2cd, the catalytic domain of the thermophilic endocellulase E2 from Thermomonospora fusca, as determined by X-ray crystallography. The structure was solved by multiple isomorphous replacement at 2.6-A resolution and has been refined at 1.8-A resolution to an R-value of 18.4% for all reflections between 10- and 1.8-A resolution. The fold of E2cd is based on an unusual parallel beta-barrel and is equivalent to the fold determined for the catalytic domain of cellobiohydrolase II, an exocellulase from Trichoderma reesei [Rouvinen et al. (1990) Science 249, 380-385]. The active site cleft of the enzyme, approximately 11 A deep and running the entire length of the molecule, is seen to be completely free for ligand binding in the crystal. A 2.2-A resolution analysis of crystals of E2cd complexed with cellobiose, an inhibitor, shows how cellobiose binds in the active site and interacts with several residues which line the cleft. Catalytic roles are suggested for three aspartic acid residues at the active site. A comparison of the E2cd and CBHIIcd structures reveals a large difference in their active site accessibilities and supports the hypothesis that the main difference between endo- and exocellulases is the degree to which their active sites are accessible to substrate.

	~~{{STRUCTURE_1tml\| PDB=1tml \| SCENE= }}~~		Crystal structure of the catalytic domain of a thermophilic endocellulase.,Spezio M, Wilson DB, Karplus PA Biochemistry. 1993 Sep 28;32(38):9906-16. PMID:8399160<ref>PMID:8399160</ref>

	~~===CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_8399160}}~~

	~~==About this Structure==~~
	~~[[1tml]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Thermobifida_fusca Thermobifida fusca]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=1TML OCA].~~

	==See Also==		==See Also==
	*[[Glucanase\|Glucanase]]		*[[Glucanase\|Glucanase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:008399160<~~/~~ref~~><~~ref group="xtra">PMID:014695246</ref><references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]