1dcp - Revision history

OCA at 06:52, 7 February 2024

2024-02-07T06:52:10Z

←Older revision		Revision as of 06:52, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. The August 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The August 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HBI:7~~,~~8-DIHYDROBIOPTERIN'>HBI</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]] 2.3Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>[https~~:~~//en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase]~~, ~~with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [https://pdbe.org/1dcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [https://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [https://pdbe.org/1dcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [https://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PHS_RAT PHS_RAT]] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>	+	[https://www.uniprot.org/uniprot/PHS_RAT PHS_RAT] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>
	== 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=1dcp 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=1dcp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DCoH, the dimerization cofactor of hepatocyte nuclear factor 1 (HNF-1), functions as both a transcriptional coactivator and a pterin dehydratase. To probe the relationship between these two functions, the X-ray crystal structures of the free enzyme and its complex with the product analogue 7,8-dihydrobiopterin were refined at 2.3 A resolution. The ligand binds at four sites per tetrameric enzyme, with little apparent conformational change in the protein. Each active-site cleft is located in a subunit interface, adjacent to a prominent saddle motif that has structural similarities to the TATA binding protein. The pterin binds within an arch of aromatic residues that extends across one dimer interface. The bound ligand makes contacts to three conserved histidines, and this arrangement restricts proposals for the enzymatic mechanism of dehydration. The dihedral symmetry of DCoH suggests that binding to the dimerization domain of HNF-1 likely involves the superposition of two-fold rotation axes of the two proteins.
-
-	High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.,Cronk JD, Endrizzi JA, Alber T Protein Sci. 1996 Oct;5(10):1963-72. PMID:8897596<ref>PMID:8897596</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dcp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: RCSB PDB Molecule of the Month]]		[[Category: RCSB PDB Molecule of the Month]]
		+	[[Category: Rattus norvegicus]]
	[[Category: Tetrahydrobiopterin Biosynthesis]]		[[Category: Tetrahydrobiopterin Biosynthesis]]
-	[[Category: Alber, T]]	+	[[Category: Alber T]]
-	[[Category: Cronk~~, J D~~]]	+	[[Category: Cronk JD]]
-	[[Category: Endrizzi~~, J A]]~~	+	[[Category: Endrizzi JA]]
-	~~[[Category: 4a-carbinolamine dehydratase]]~~	+
-	~~[[Category: Dehydratase]]~~	+
-	~~[[Category: Dimerization cofactor]]~~	+
-	~~[[Category: Transcriptional stimulator]]~~	+
-	~~[[Category: Transregulator of homeodomain protein~~]]	+

OCA at 10:45, 14 July 2021

2021-07-14T10:45:17Z

←Older revision		Revision as of 10:45, 14 July 2021
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	<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The August 2015 RCSB PDB [~~http~~://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [~~http~~://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DCP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The August 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [~~http~~://pdbe.org/1dcp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [https://pdbe.org/1dcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [https://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PHS_RAT PHS_RAT]] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>	+	[[https://www.uniprot.org/uniprot/PHS_RAT PHS_RAT]] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:43, 10 October 2019

2019-10-10T06:43:14Z

←Older revision		Revision as of 06:43, 10 October 2019
Line 1:		Line 1:

	==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==		==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==
-	<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1dcp' size='340' side='right'caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The August 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The August 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
Line 35:		Line 35:
	[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]		[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: RCSB PDB Molecule of the Month]]		[[Category: RCSB PDB Molecule of the Month]]
	[[Category: Tetrahydrobiopterin Biosynthesis]]		[[Category: Tetrahydrobiopterin Biosynthesis]]

OCA at 08:23, 6 December 2017

2017-12-06T08:23:28Z

←Older revision		Revision as of 08:23, 6 December 2017
Line 1:		Line 1:
		+
	==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==		==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==
	<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://pdbe.org/1dcp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://pdbe.org/1dcp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcp_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 05:54, 10 February 2016

2016-02-10T05:54:52Z

←Older revision		Revision as of 05:54, 10 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=1dcp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:00, 11 September 2015

2015-09-11T06:00:52Z

←Older revision		Revision as of 06:00, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The August 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Tetrahydrobiopterin Biosynthesis'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_8 10.2210/rcsb_pdb/mom_2015_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://pdbe.org/1dcp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 1dcp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]		[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
		+	[[Category: RCSB PDB Molecule of the Month]]
		+	[[Category: Tetrahydrobiopterin Biosynthesis]]
	[[Category: Alber, T]]		[[Category: Alber, T]]
	[[Category: Cronk, J D]]		[[Category: Cronk, J D]]

OCA at 12:16, 25 December 2014

2014-12-25T12:16:29Z

←Older revision		Revision as of 12:16, 25 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PHS_RAT PHS_RAT]] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 20:09, 22 December 2014

2014-12-22T20:09:24Z

←Older revision		Revision as of 20:09, 22 December 2014
Line 31:		Line 31:
	[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]		[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Alber, T.]]	+	[[Category: Alber, T]]
-	[[Category: Cronk, J D.]]	+	[[Category: Cronk, J D]]
-	[[Category: Endrizzi, J A.]]	+	[[Category: Endrizzi, J A]]
	[[Category: 4a-carbinolamine dehydratase]]		[[Category: 4a-carbinolamine dehydratase]]
	[[Category: Dehydratase]]		[[Category: Dehydratase]]

OCA at 05:51, 10 October 2014

2014-10-10T05:51:52Z

←Older revision		Revision as of 05:51, 10 October 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp 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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:35, 4 September 2014

2014-09-04T06:35:07Z

←Older revision		Revision as of 06:35, 4 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1dcp.~~png\|left~~\|200px]]	+	==DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN==
		+	<StructureSection load='1dcp' size='340' side='right' caption='[[1dcp]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dcp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=1dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dcp RCSB], [http://www.ebi.ac.uk/pdbsum/1dcp 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/dc/1dcp_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 ==
		+	DCoH, the dimerization cofactor of hepatocyte nuclear factor 1 (HNF-1), functions as both a transcriptional coactivator and a pterin dehydratase. To probe the relationship between these two functions, the X-ray crystal structures of the free enzyme and its complex with the product analogue 7,8-dihydrobiopterin were refined at 2.3 A resolution. The ligand binds at four sites per tetrameric enzyme, with little apparent conformational change in the protein. Each active-site cleft is located in a subunit interface, adjacent to a prominent saddle motif that has structural similarities to the TATA binding protein. The pterin binds within an arch of aromatic residues that extends across one dimer interface. The bound ligand makes contacts to three conserved histidines, and this arrangement restricts proposals for the enzymatic mechanism of dehydration. The dihedral symmetry of DCoH suggests that binding to the dimerization domain of HNF-1 likely involves the superposition of two-fold rotation axes of the two proteins.

-	~~{{STRUCTURE_1dcp\| PDB=1dcp \| SCENE= }}~~	+	High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.,Cronk JD, Endrizzi JA, Alber T Protein Sci. 1996 Oct;5(10):1963-72. PMID:8897596<ref>PMID:8897596</ref>

-	~~===DCOH~~, ~~A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8897596}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1dcp]] is~~ a ~~8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1DCP OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:008897596<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]		[[Category: 4a-hydroxytetrahydrobiopterin dehydratase]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]