1cbh - Revision history

OCA at 15:38, 13 March 2024

OCA — Wed, 13 Mar 2024 15:38:49 GMT

←Older revision		Revision as of 15:38, 13 March 2024
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	==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==		==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==
-	<StructureSection load='1cbh' size='340' side='right'caption='[[1cbh~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1cbh' size='340' side='right'caption='[[1cbh]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_13631 Atcc 13631~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CBH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[2cbh\|2cbh]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [https://pdbe.org/1cbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [https://www.ebi.ac.uk/pdbsum/1cbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [https://pdbe.org/1cbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [https://www.ebi.ac.uk/pdbsum/1cbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.	+	[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
	== 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=1cbh 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=1cbh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The solution structure of a synthetic 36-residue polypeptide comprising the C-terminal cellulose binding domain of cellobiohydrolase I (CT-CBH I) from Trichoderma reesei was investigated by nuclear magnetic resonance (NMR) spectroscopy. The 1H NMR spectrum was completely assigned in a sequential manner by two-dimensional NMR techniques. A large number of stereospecific assignments for beta-methylene protons, as well as ranges for the phi, psi, and chi 1 torsion angles, were obtained on the basis of sequential and intraresidue nuclear Overhauser enhancement (NOE) and coupling constant data in combination with a conformational data base search. The structure calculations were carried out in an iterative manner by using the hybrid distance geometry-dynamical simulated annealing method. This involved computing a series of initial structures from a subset of the experimental data in order to resolve ambiguities in the assignments of some NOE cross-peaks arising from chemical shift degeneracy. Additionally, this permitted us to extend the stereospecific assignments to the alpha-methylene protons of glycine using information on phi torsion angles derived from the initial structure calculations. The final experimental data set consisted of 554 interproton distance restraints, 24 restraints for 12 hydrogen bonds, and 33 phi, 24 psi, and 25 chi 1 torsion angle restraints. CT-CBH I has two disulfide bridges whose pairing was previously unknown. Analysis of structures calculated with all three possible combinations of disulfide bonds, as well as without disulfide bonds, indicated that the correct disulfide bridge pairing was 8-25 and 19-35. Forty-one structures were computed with the 8-25 and 19-35 disulfide bridges, and the average atomic rms difference between the individual structures and the mean structure obtained by averaging their coordinates was 0.33 +/- 0.04 A for the backbone atoms and 0.52 +/- 0.06 A for all atoms. The protein has a wedgelike shape with an amphiphilic character, one face being predominantly hydrophilic and the other mainly hydrophobic. The principal element of secondary structure is made up of an irregular triple-stranded antiparallel beta-sheet composed of residues 5-9 (beta 1), 24-28 (beta 2), and 33-36 (beta 3) in which strand beta 3 is hydrogen bonded to the other two strands.(ABSTRACT TRUNCATED AT 400 WORDS)
-
-	Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.,Kraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM Biochemistry. 1989 Sep 5;28(18):7241-57. PMID:2554967<ref>PMID:2554967</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1cbh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]		*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 13631]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Clore~~, G M~~]]	+	[[Category: Trichoderma reesei]]
-	[[Category: Gronenborn~~, A M~~]]	+	[[Category: Clore GM]]
		+	[[Category: Gronenborn AM]]

OCA at 10:35, 14 July 2021

OCA — Wed, 14 Jul 2021 10:35:07 GMT

←Older revision		Revision as of 10:35, 14 July 2021
Line 3:		Line 3:
	<StructureSection load='1cbh' size='340' side='right'caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cbh' size='340' side='right'caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1CBH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cbh\|2cbh]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [~~http~~://pdbe.org/1cbh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1cbh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [https://pdbe.org/1cbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [https://www.ebi.ac.uk/pdbsum/1cbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.	+	[[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:02, 10 October 2019

OCA — Thu, 10 Oct 2019 07:02:02 GMT

←Older revision		Revision as of 07:02, 10 October 2019
Line 1:		Line 1:

	==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==		==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==
-	<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1cbh' size='340' side='right'caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/1cbh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/1cbh_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>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1cbh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cbh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Atcc 13631]]		[[Category: Atcc 13631]]
		+	[[Category: Large Structures]]
	[[Category: Clore, G M]]		[[Category: Clore, G M]]
	[[Category: Gronenborn, A M]]		[[Category: Gronenborn, A M]]

OCA at 10:59, 8 November 2017

OCA — Wed, 08 Nov 2017 10:59:45 GMT

←Older revision		Revision as of 10:59, 8 November 2017
Line 1:		Line 1:
		+
	==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==		==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==
	<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://pdbe.org/1cbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://pdbe.org/1cbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1cbh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cbh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cellobiohydrolase\|Cellobiohydrolase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 23:02, 7 February 2016

OCA — Sun, 07 Feb 2016 23:02:29 GMT

←Older revision		Revision as of 23:02, 7 February 2016
Line 17:		Line 17:
	<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=1cbh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:40, 10 September 2015

OCA — Thu, 10 Sep 2015 05:40:23 GMT

←Older revision		Revision as of 05:40, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Trichoderma_reesei Trichoderma reesei~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-~~cellobiosidase~~ Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://pdbe.org/1cbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~GUX1_TRIRE GUX1_TRIRE~~]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.	+	[[http://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 27:
	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 1cbh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cellulose 1,4-beta-cellobiosidase]]~~	+	[[Category: Atcc 13631]]
-	~~[[Category: Trichoderma reesei~~]]	+
	[[Category: Clore, G M]]		[[Category: Clore, G M]]
	[[Category: Gronenborn, A M]]		[[Category: Gronenborn, A M]]

OCA at 18:48, 24 December 2014

OCA — Wed, 24 Dec 2014 18:48:37 GMT

←Older revision		Revision as of 18:48, 24 December 2014
Line 7:		Line 7:
	<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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GUX1_TRIRE GUX1_TRIRE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:55, 22 December 2014

OCA — Mon, 22 Dec 2014 10:55:46 GMT

←Older revision		Revision as of 10:55, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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: Cellulose 1,4-beta-cellobiosidase]]		[[Category: Cellulose 1,4-beta-cellobiosidase]]
	[[Category: Trichoderma reesei]]		[[Category: Trichoderma reesei]]
-	[[Category: Clore, G M.]]	+	[[Category: Clore, G M]]
-	[[Category: Gronenborn, A M.]]	+	[[Category: Gronenborn, A M]]

OCA at 17:14, 20 August 2014

OCA — Wed, 20 Aug 2014 17:14:50 GMT

←Older revision		Revision as of 17:14, 20 August 2014
Line 1:		Line 1:
-	[[~~Image:~~1cbh.~~png~~\|~~left~~\|200px]]	+	==DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==
		+	<StructureSection load='1cbh' size='340' side='right' caption='[[1cbh]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CBH FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2cbh\|2cbh]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cbh RCSB], [http://www.ebi.ac.uk/pdbsum/1cbh 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/cb/1cbh_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 ==
		+	The solution structure of a synthetic 36-residue polypeptide comprising the C-terminal cellulose binding domain of cellobiohydrolase I (CT-CBH I) from Trichoderma reesei was investigated by nuclear magnetic resonance (NMR) spectroscopy. The 1H NMR spectrum was completely assigned in a sequential manner by two-dimensional NMR techniques. A large number of stereospecific assignments for beta-methylene protons, as well as ranges for the phi, psi, and chi 1 torsion angles, were obtained on the basis of sequential and intraresidue nuclear Overhauser enhancement (NOE) and coupling constant data in combination with a conformational data base search. The structure calculations were carried out in an iterative manner by using the hybrid distance geometry-dynamical simulated annealing method. This involved computing a series of initial structures from a subset of the experimental data in order to resolve ambiguities in the assignments of some NOE cross-peaks arising from chemical shift degeneracy. Additionally, this permitted us to extend the stereospecific assignments to the alpha-methylene protons of glycine using information on phi torsion angles derived from the initial structure calculations. The final experimental data set consisted of 554 interproton distance restraints, 24 restraints for 12 hydrogen bonds, and 33 phi, 24 psi, and 25 chi 1 torsion angle restraints. CT-CBH I has two disulfide bridges whose pairing was previously unknown. Analysis of structures calculated with all three possible combinations of disulfide bonds, as well as without disulfide bonds, indicated that the correct disulfide bridge pairing was 8-25 and 19-35. Forty-one structures were computed with the 8-25 and 19-35 disulfide bridges, and the average atomic rms difference between the individual structures and the mean structure obtained by averaging their coordinates was 0.33 +/- 0.04 A for the backbone atoms and 0.52 +/- 0.06 A for all atoms. The protein has a wedgelike shape with an amphiphilic character, one face being predominantly hydrophilic and the other mainly hydrophobic. The principal element of secondary structure is made up of an irregular triple-stranded antiparallel beta-sheet composed of residues 5-9 (beta 1), 24-28 (beta 2), and 33-36 (beta 3) in which strand beta 3 is hydrogen bonded to the other two strands.(ABSTRACT TRUNCATED AT 400 WORDS)

-	~~{{STRUCTURE_1cbh\| PDB=1cbh \| SCENE= }}~~	+	Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.,Kraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM Biochemistry. 1989 Sep 5;28(18):7241-57. PMID:2554967<ref>PMID:2554967</ref>

-	===DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING===	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_2554967}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1cbh]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Trichoderma_reesei Trichoderma reesei]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA].~~	+

	==See Also==		==See Also==
	*[[Cellobiohydrolase\|Cellobiohydrolase]]		*[[Cellobiohydrolase\|Cellobiohydrolase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:002554967<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cellulose 1,4-beta-cellobiosidase]]		[[Category: Cellulose 1,4-beta-cellobiosidase]]
	[[Category: Trichoderma reesei]]		[[Category: Trichoderma reesei]]
	[[Category: Clore, G M.]]		[[Category: Clore, G M.]]
	[[Category: Gronenborn, A M.]]		[[Category: Gronenborn, A M.]]

OCA at 08:06, 20 October 2012

OCA — Sat, 20 Oct 2012 08:06:06 GMT

←Older revision		Revision as of 08:06, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1cbh]] is a 1 chain structure ~~of [[Cellobiohydrolase]]~~ with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA].	+	[[1cbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBH OCA].

	==See Also==		==See Also==
Line 14:		Line 14:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:002554967~~</ref><ref group="xtra">PMID:011734033~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:002554967</ref><references group="xtra"/>
	[[Category: Cellulose 1,4-beta-cellobiosidase]]		[[Category: Cellulose 1,4-beta-cellobiosidase]]
	[[Category: Trichoderma reesei]]		[[Category: Trichoderma reesei]]
	[[Category: Clore, G M.]]		[[Category: Clore, G M.]]
	[[Category: Gronenborn, A M.]]		[[Category: Gronenborn, A M.]]