2man - Revision history

OCA at 06:28, 3 April 2024

OCA — Wed, 03 Apr 2024 06:28:22 GMT

←Older revision		Revision as of 06:28, 3 April 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BMA:BETA~~-~~D-MANNOSE'>BMA</scene>~~, ~~<scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 1.9Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https:~~/~~/en.wikipedia.org/wiki/Mannan_endo-1~~,4-~~beta~~-~~mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [https://pdbe.org/2man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [https://www.ebi.ac.uk/pdbsum/2man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2man 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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [https://pdbe.org/2man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [https://www.ebi.ac.uk/pdbsum/2man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2man ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q9ZF13_THEFU Q9ZF13_THEFU]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 20:
	</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=2man 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=2man ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Background:. beta-Mannanases hydrolyse the O-glycosidic bonds in mannan, a hemicellulose constituent of plants. These enzymes have potential use in pulp and paper production and are of significant biotechnological interest. Thermostable beta-mannanases would be particularly useful due to their high temperature optimum and broad pH tolerance. The thermophilic actinomycete Thermomonospora fusca secretes at least one beta-mannanase (molecular mass 38 kDa) with a temperature optimum of 80 degreesC. No three-dimensional structure of a mannan-degrading enzyme has been reported until now. Results:. The crystal structure of the thermostable beta-mannanase from T. fusca has been determined by the multiple isomorphous replacement method and refined to 1.5 A resolution. In addition to the native enzyme, the structures of the mannotriose- and mannohexaose-bound forms of the enzyme have been determined to resolutions of 1.9 A and 1.6 A, respectively. Conclusions:. Analysis of the -1 subsite of T. fusca mannanase reveals neither a favourable interaction towards the axial HO-C(2) nor a discrimination against the equatorial hydroxyl group of gluco-configurated substrates. We propose that selectivity arises from two possible mechanisms: a hydrophobic interaction of the substrate with Val263, conserved in family 5 bacterial mannanases, which discriminates between the different conformations of the hydroxymethyl group in native mannan and cellulose; and/or a specific interaction between Asp259 and the axial hydroxyl group at the C(2) of the substrate in the -2 subsite. Compared with the catalytic clefts of family 5 cellulases, the groove of T. fusca mannanase has a strongly reduced number of aromatic residues providing platforms for stacking with the substrate. This deletion of every second platform is in good agreement with the orientation of the axial hydroxyl groups in mannan.
-
-	High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5.,Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD, Zimmermann W, Winterhalter K, Piontek K Structure. 1998 Nov 15;6(11):1433-44. PMID:9817845<ref>PMID:9817845</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2man" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Mannan endo-1,4-beta-mannosidase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]
-	[[Category: Gloor~~, S M~~]]	+	[[Category: Gloor SM]]
-	[[Category: Hilge, M]]	+	[[Category: Hilge M]]
-	[[Category: Piontek, K]]	+	[[Category: Piontek K]]
-	~~[[Category: Family 5]]~~	+
-	~~[[Category: Glycosyl hydrolase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mannanase]]~~	+
-	~~[[Category: Thermomonospora fusca~~]]	+

OCA at 11:34, 16 February 2022

OCA — Wed, 16 Feb 2022 11:34:17 GMT

←Older revision		Revision as of 11:34, 16 February 2022
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	<StructureSection load='2man' size='340' side='right'caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2man' size='340' side='right'caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2MAN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [~~http~~://pdbe.org/2man PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2man PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2man 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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [https://pdbe.org/2man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [https://www.ebi.ac.uk/pdbsum/2man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2man ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 06:21, 13 May 2020

OCA — Wed, 13 May 2020 06:21:14 GMT

←Older revision		Revision as of 06:21, 13 May 2020
Line 1:		Line 1:

	==MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE==		==MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE==
-	<StructureSection load='2man' size='340' side='right' caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='2man' size='340' side='right'caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MAN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2MAN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://pdbe.org/2man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2man ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://pdbe.org/2man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2man ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Mannan endo-1,4-beta-mannosidase]]		[[Category: Mannan endo-1,4-beta-mannosidase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]

OCA at 22:49, 9 August 2018

OCA — Thu, 09 Aug 2018 22:49:16 GMT

←Older revision		Revision as of 22:49, 9 August 2018
Line 1:		Line 1:
		+
	==MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE==		==MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE==
	<StructureSection load='2man' size='340' side='right' caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2man' size='340' side='right' caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://pdbe.org/2man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://pdbe.org/2man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2man 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/ma/2man_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/2man_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>
	</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=2man ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 16:02, 11 September 2015

OCA — Fri, 11 Sep 2015 16:02:35 GMT

←Older revision		Revision as of 16:02, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://pdbe.org/2man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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 2man" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:48, 19 January 2015

OCA — Mon, 19 Jan 2015 17:48:04 GMT

←Older revision		Revision as of 17:48, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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 31:		Line 31:
	[[Category: Mannan endo-1,4-beta-mannosidase]]		[[Category: Mannan endo-1,4-beta-mannosidase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]
-	[[Category: Gloor, S M.]]	+	[[Category: Gloor, S M]]
-	[[Category: Hilge, M.]]	+	[[Category: Hilge, M]]
-	[[Category: Piontek, K.]]	+	[[Category: Piontek, K]]
	[[Category: Family 5]]		[[Category: Family 5]]
	[[Category: Glycosyl hydrolase]]		[[Category: Glycosyl hydrolase]]

OCA at 20:04, 30 September 2014

OCA — Tue, 30 Sep 2014 20:04:05 GMT

←Older revision		Revision as of 20:04, 30 September 2014
Line 1:		Line 1:
-	[[~~Image~~:2man.~~png\|left~~\|200px]]	+	==MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE==
		+	<StructureSection load='2man' size='340' side='right' caption='[[2man]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2man]] 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=2MAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAN FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=2man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2man OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2man RCSB], [http://www.ebi.ac.uk/pdbsum/2man 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/ma/2man_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 ==
		+	Background:. beta-Mannanases hydrolyse the O-glycosidic bonds in mannan, a hemicellulose constituent of plants. These enzymes have potential use in pulp and paper production and are of significant biotechnological interest. Thermostable beta-mannanases would be particularly useful due to their high temperature optimum and broad pH tolerance. The thermophilic actinomycete Thermomonospora fusca secretes at least one beta-mannanase (molecular mass 38 kDa) with a temperature optimum of 80 degreesC. No three-dimensional structure of a mannan-degrading enzyme has been reported until now. Results:. The crystal structure of the thermostable beta-mannanase from T. fusca has been determined by the multiple isomorphous replacement method and refined to 1.5 A resolution. In addition to the native enzyme, the structures of the mannotriose- and mannohexaose-bound forms of the enzyme have been determined to resolutions of 1.9 A and 1.6 A, respectively. Conclusions:. Analysis of the -1 subsite of T. fusca mannanase reveals neither a favourable interaction towards the axial HO-C(2) nor a discrimination against the equatorial hydroxyl group of gluco-configurated substrates. We propose that selectivity arises from two possible mechanisms: a hydrophobic interaction of the substrate with Val263, conserved in family 5 bacterial mannanases, which discriminates between the different conformations of the hydroxymethyl group in native mannan and cellulose; and/or a specific interaction between Asp259 and the axial hydroxyl group at the C(2) of the substrate in the -2 subsite. Compared with the catalytic clefts of family 5 cellulases, the groove of T. fusca mannanase has a strongly reduced number of aromatic residues providing platforms for stacking with the substrate. This deletion of every second platform is in good agreement with the orientation of the axial hydroxyl groups in mannan.

-	~~{{STRUCTURE_2man\| PDB=2man \| SCENE= }}~~	+	High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5.,Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD, Zimmermann W, Winterhalter K, Piontek K Structure. 1998 Nov 15;6(11):1433-44. PMID:9817845<ref>PMID:9817845</ref>

-	~~===MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9817845}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2man]] 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=2MAN OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:009817845<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mannan endo-1,4-beta-mannosidase]]		[[Category: Mannan endo-1,4-beta-mannosidase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]

OCA: Protected "2man" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 15:05:33 GMT

Protected "2man" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:05, 7 January 2013

OCA at 15:05, 7 January 2013

OCA — Mon, 07 Jan 2013 15:05:31 GMT

←Older revision		Revision as of 15:05, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2man.png\|left\|200px]]		[[Image:2man.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2man", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2man\| PDB=2man \| SCENE= }}		{{STRUCTURE_2man\| PDB=2man \| SCENE= }}

	===MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE===		===MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9817845}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9817845 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9817845}}		{{ABSTRACT_PUBMED_9817845}}

	==About this Structure==		==About this Structure==
-	~~2MAN~~ is a 1 chain structure of 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=2MAN OCA].	+	[[2man]] 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=2MAN OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9817845~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009817845</ref><references group="xtra"/>
	[[Category: Mannan endo-1,4-beta-mannosidase]]		[[Category: Mannan endo-1,4-beta-mannosidase]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]
Line 31:		Line 19:
	[[Category: Family 5]]		[[Category: Family 5]]
	[[Category: Glycosyl hydrolase]]		[[Category: Glycosyl hydrolase]]
		+	[[Category: Hydrolase]]
	[[Category: Mannanase]]		[[Category: Mannanase]]
	[[Category: Thermomonospora fusca]]		[[Category: Thermomonospora fusca]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:54:12 2009''

OCA at 00:54, 18 February 2009

OCA — Wed, 18 Feb 2009 00:54:14 GMT

←Older revision		Revision as of 00:54, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2MAN is a ~~[[Single protein]]~~ structure of 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=2MAN OCA].	+	2MAN is a 1 chain structure of 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=2MAN OCA].

	==Reference==		==Reference==
-	High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5., Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD, Zimmermann W, Winterhalter K, Piontek K, Structure. 1998 Nov 15;6(11):1433-44. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9817845 9817845]~~	+	<ref group="xtra">PMID:9817845</ref><references group="xtra"/>
	[[Category: Mannan endo-1,4-beta-mannosidase]]		[[Category: Mannan endo-1,4-beta-mannosidase]]
-	[[Category: Single protein]]
	[[Category: Thermobifida fusca]]		[[Category: Thermobifida fusca]]
	[[Category: Gloor, S M.]]		[[Category: Gloor, S M.]]
Line 35:		Line 34:
	[[Category: Thermomonospora fusca]]		[[Category: Thermomonospora fusca]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 09~~:34:~~41 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:54:12 2009''