4c8h - Revision history

OCA at 17:32, 7 September 2022

2022-09-07T17:32:12Z

←Older revision		Revision as of 17:32, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c8h' size='340' side='right'caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='4c8h' size='340' side='right'caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C8H FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C8H FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [~~http~~://pdbe.org/4c8h PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c8h PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8h 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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [https://pdbe.org/4c8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [https://www.ebi.ac.uk/pdbsum/4c8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8h ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST]] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.	+	[[https://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST]] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Efficient duplication of the genome requires the concerted action of helicase and DNA polymerases at replication forks to avoid stalling of the replication machinery and consequent genomic instability. In eukaryotes, the physical coupling between helicase and DNA polymerases remains poorly understood. Here we define the molecular mechanism by which the yeast Ctf4 protein links the Cdc45-MCM-GINS (CMG) DNA helicase to DNA polymerase alpha (Pol alpha) within the replisome. We use X-ray crystallography and electron microscopy to show that Ctf4 self-associates in a constitutive disk-shaped trimer. Trimerization depends on a beta-propeller domain in the carboxy-terminal half of the protein, which is fused to a helical extension that protrudes from one face of the trimeric disk. Critically, Pol alpha and the CMG helicase share a common mechanism of interaction with Ctf4. We show that the amino-terminal tails of the catalytic subunit of Pol alpha and the Sld5 subunit of GINS contain a conserved Ctf4-binding motif that docks onto the exposed helical extension of a Ctf4 protomer within the trimer. Accordingly, we demonstrate that one Ctf4 trimer can support binding of up to three partner proteins, including the simultaneous association with both Pol alpha and GINS. Our findings indicate that Ctf4 can couple two molecules of Pol alpha to one CMG helicase within the replisome, providing a new model for lagging-strand synthesis in eukaryotes that resembles the emerging model for the simpler replisome of Escherichia coli. The ability of Ctf4 to act as a platform for multivalent interactions illustrates a mechanism for the concurrent recruitment of factors that act together at the fork.	+
-		+
-	A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome.,Simon AC, Zhou JC, Perera RL, van Deursen F, Evrin C, Ivanova ME, Kilkenny ML, Renault L, Kjaer S, Matak-Vinkovic D, Labib K, Costa A, Pellegrini L Nature. 2014 May 4. doi: 10.1038/nature13234. PMID:24805245<ref>PMID:24805245</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c8h" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pellegrini, L~~]]	+	[[Category: Saccharomyces cerevisiae]]
-	[[Category: ~~Simon, A C~~]]	+	[[Category: Pellegrini L]]
-	[[Category: ~~Adaptor protein]]~~	+	[[Category: Simon AC]]
-	~~[[Category: Beta propeller domain]]~~	+
-	~~[[Category: Dna replication~~]]	+

OCA at 09:48, 20 March 2019

2019-03-20T09:48:49Z

←Older revision		Revision as of 09:48, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein.==		==Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein.==
-	<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>	+	<StructureSection load='4c8h' size='340' side='right'caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
		+	[[Category: Large Structures]]
	[[Category: Pellegrini, L]]		[[Category: Pellegrini, L]]
	[[Category: Simon, A C]]		[[Category: Simon, A C]]

OCA at 20:55, 4 August 2016

2016-08-04T20:55:37Z

←Older revision		Revision as of 20:55, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein.==		==Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein.==
	<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h 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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://pdbe.org/4c8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8h ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4c8h" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:34, 24 December 2014

2014-12-24T19:34:25Z

←Older revision		Revision as of 19:34, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h 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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST]] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
-	[[Category: Pellegrini, L.]]	+	[[Category: Pellegrini, L]]
-	[[Category: Simon, A C.]]	+	[[Category: Simon, A C]]
	[[Category: Adaptor protein]]		[[Category: Adaptor protein]]
	[[Category: Beta propeller domain]]		[[Category: Beta propeller domain]]
	[[Category: Dna replication]]		[[Category: Dna replication]]

OCA at 05:25, 18 June 2014

2014-06-18T05:25:37Z

←Older revision		Revision as of 05:25, 18 June 2014
Line 12:		Line 12:
	A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome.,Simon AC, Zhou JC, Perera RL, van Deursen F, Evrin C, Ivanova ME, Kilkenny ML, Renault L, Kjaer S, Matak-Vinkovic D, Labib K, Costa A, Pellegrini L Nature. 2014 May 4. doi: 10.1038/nature13234. PMID:24805245<ref>PMID:24805245</ref>		A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome.,Simon AC, Zhou JC, Perera RL, van Deursen F, Evrin C, Ivanova ME, Kilkenny ML, Renault L, Kjaer S, Matak-Vinkovic D, Labib K, Costa A, Pellegrini L Nature. 2014 May 4. doi: 10.1038/nature13234. PMID:24805245<ref>PMID:24805245</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==

OCA at 06:51, 21 May 2014

2014-05-21T06:51:07Z

←Older revision		Revision as of 06:51, 21 May 2014
Line 2:		Line 2:
	<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>	+	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C8H FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Efficient duplication of the genome requires the concerted action of helicase and DNA polymerases at replication forks to avoid stalling of the replication machinery and consequent genomic instability. In eukaryotes, the physical coupling between helicase and DNA polymerases remains poorly understood. Here we define the molecular mechanism by which the yeast Ctf4 protein links the Cdc45-MCM-GINS (CMG) DNA helicase to DNA polymerase alpha (Pol alpha) within the replisome. We use X-ray crystallography and electron microscopy to show that Ctf4 self-associates in a constitutive disk-shaped trimer. Trimerization depends on a beta-propeller domain in the carboxy-terminal half of the protein, which is fused to a helical extension that protrudes from one face of the trimeric disk. Critically, Pol alpha and the CMG helicase share a common mechanism of interaction with Ctf4. We show that the amino-terminal tails of the catalytic subunit of Pol alpha and the Sld5 subunit of GINS contain a conserved Ctf4-binding motif that docks onto the exposed helical extension of a Ctf4 protomer within the trimer. Accordingly, we demonstrate that one Ctf4 trimer can support binding of up to three partner proteins, including the simultaneous association with both Pol alpha and GINS. Our findings indicate that Ctf4 can couple two molecules of Pol alpha to one CMG helicase within the replisome, providing a new model for lagging-strand synthesis in eukaryotes that resembles the emerging model for the simpler replisome of Escherichia coli. The ability of Ctf4 to act as a platform for multivalent interactions illustrates a mechanism for the concurrent recruitment of factors that act together at the fork.
		+
		+	A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome.,Simon AC, Zhou JC, Perera RL, van Deursen F, Evrin C, Ivanova ME, Kilkenny ML, Renault L, Kjaer S, Matak-Vinkovic D, Labib K, Costa A, Pellegrini L Nature. 2014 May 4. doi: 10.1038/nature13234. PMID:24805245<ref>PMID:24805245</ref>
		+
		+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 18824]]
	[[Category: Pellegrini, L.]]		[[Category: Pellegrini, L.]]
	[[Category: Simon, A C.]]		[[Category: Simon, A C.]]

OCA at 09:19, 1 May 2014

2014-05-01T09:19:32Z

←Older revision		Revision as of 09:19, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>		<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>	+	<table><tr><td colspan='2'>[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>
-	<b>[[Non-Standard_Residue\|NonStd Res:]]</b> <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</span><br>	+	<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=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</span></td></tr>
		+	<table>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:51, 30 April 2014

2014-04-30T09:51:38Z

←Older revision		Revision as of 09:51, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>		[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>
		+	<b>[[Non-Standard_Residue\|NonStd Res:]]</b> <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c8h RCSB], [http://www.ebi.ac.uk/pdbsum/4c8h PDBsum]</span><br>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:56, 30 April 2014

2014-04-30T07:56:54Z

←Older revision		Revision as of 07:56, 30 April 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein.==
-		+	<StructureSection load='4c8h' size='340' side='right' caption='[[4c8h]], [[Resolution\|resolution]] 2.69Å' scene=''>
-	~~The entry~~ 4c8h is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	[[4c8h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8H OCA]. <br>
-	~~Authors~~: ~~Simon, A~~.C., Pellegrini, L.	+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
-		+	== References ==
-	~~Description~~:	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Pellegrini, L.]]
		+	[[Category: Simon, A C.]]
		+	[[Category: Adaptor protein]]
		+	[[Category: Beta propeller domain]]
		+	[[Category: Dna replication]]

OCA at 07:08, 16 October 2013

2013-10-16T07:08:31Z

←Older revision		Revision as of 07:08, 16 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c8h is ON HOLD	+	The entry 4c8h is ON HOLD until Paper Publication

	Authors: Simon, A.C., Pellegrini, L.		Authors: Simon, A.C., Pellegrini, L.

	Description:		Description: