2m45 - Revision history

OCA at 13:28, 22 February 2023

2023-02-22T13:28:29Z

←Older revision		Revision as of 13:28, 22 February 2023
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	==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==		==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
-	<StructureSection load='2m45' size='340' side='right'caption='[[2m45~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2m45' size='340' side='right'caption='[[2m45]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2m45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Sulso Sulso~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M45 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M45 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>	+	</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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [https://pdbe.org/2m45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [https://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [https://pdbe.org/2m45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [https://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~MCM_SULSO MCM_SULSO]~~] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>	+	[https://www.uniprot.org/uniprot/MCM_SACS2 MCM_SACS2] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: DNA helicase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Sulso~~]]	+	[[Category: Saccharolobus solfataricus P2]]
-	[[Category: Gorlach, M]]	+	[[Category: Gorlach M]]
-	[[Category: Medagli, B]]	+	[[Category: Medagli B]]
-	[[Category: Ohlenschlager, O]]	+	[[Category: Ohlenschlager O]]
-	[[Category: Onesti, S]]	+	[[Category: Onesti S]]
-	[[Category: Wiedemann, C]]	+	[[Category: Wiedemann C]]
-	~~[[Category: Dna helicase]]~~	+
-	~~[[Category: Helix-turn-helix]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mcm]]~~	+
-	~~[[Category: Minichromosome maintenance protein]]~~	+
-	~~[[Category: Pre-replicative complex]]~~	+
-	~~[[Category: Replication]]~~	+
-	~~[[Category: Thermophile protein]]~~	+
-	~~[[Category: Winged helix]]~~	+
-	~~[[Category: Winged helix turn~~]]	+

OCA at 10:59, 19 May 2021

2021-05-19T10:59:12Z

←Older revision		Revision as of 10:59, 19 May 2021
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	==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==		==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
-	<StructureSection load='2m45' size='340' side='right' caption='[[2m45]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2m45' size='340' side='right'caption='[[2m45]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2m45]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Sulso Sulso]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2M45 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulso Sulso]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M45 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [~~http~~://pdbe.org/2m45 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [https://pdbe.org/2m45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [https://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>	+	[[https://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
		+	[[Category: Large Structures]]
	[[Category: Sulso]]		[[Category: Sulso]]
	[[Category: Gorlach, M]]		[[Category: Gorlach, M]]

OCA at 17:29, 9 March 2017

2017-03-09T17:29:22Z

←Older revision		Revision as of 17:29, 9 March 2017
Line 1:		Line 1:
		+
	==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==		==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
	<StructureSection load='2m45' size='340' side='right' caption='[[2m45]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2m45' size='340' side='right' caption='[[2m45]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://pdbe.org/2m45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m45 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 2m45" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:17, 20 May 2015

2015-05-20T06:17:55Z

←Older revision		Revision as of 06:17, 20 May 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>		[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The minichromosome maintenance complex (MCM) represents the replicative DNA helicase both in eukaryotes and archaea. Here, we describe the solution structure of the C-terminal domains of the archaeal MCMs of Sulfolobus solfataricus (Sso) and Methanothermobacter thermautotrophicus (Mth). Those domains consist of a structurally conserved truncated winged helix (WH) domain lacking the two typical 'wings' of canonical WH domains. A less conserved N-terminal extension links this WH module to the MCM AAA+ domain forming the ATPase center. In the Sso MCM this linker contains a short alpha-helical element. Using Sso MCM mutants, including chimeric constructs containing Mth C-terminal domain elements, we show that the ATPase and helicase activity of the Sso MCM is significantly modulated by the short alpha-helical linker element and by N-terminal residues of the first alpha-helix of the truncated WH module. Finally, based on our structural and functional data, we present a docking-derived model of the Sso MCM, which implies an allosteric control of the ATPase center by the C-terminal domain.
		+
		+	Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex.,Wiedemann C, Szambowska A, Hafner S, Ohlenschlager O, Guhrs KH, Gorlach M Nucleic Acids Res. 2015 Mar 11;43(5):2958-67. doi: 10.1093/nar/gkv120. Epub 2015 , Feb 20. PMID:25712103<ref>PMID:25712103</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:20, 24 December 2014

2014-12-24T16:20:12Z

←Older revision		Revision as of 16:20, 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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:22, 21 December 2014

2014-12-21T17:22:41Z

←Older revision		Revision as of 17:22, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2m45\| PDB=2m45 \| SCENE= }}~~	+	==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
-	===NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus===	+	<StructureSection load='2m45' size='340' side='right' caption='[[2m45]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-		+	== Structural highlights ==
-	==~~Function~~==	+	<table><tr><td colspan='2'>[[2m45]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M45 FirstGlance]. <br>
-	[[~~http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO~~]] ~~Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5~~'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>~~PMID:11821426</ref>~~	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MCM, SSO0774 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
-	==~~About this Structure~~==	+	<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=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum]</span></td></tr>
-	[[2m45]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA].	+	</table>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~references group~~="~~xtra~~"/><~~references~~/>	+
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
-	[[Category: Gorlach, M.]]	+	[[Category: Sulso]]
-	[[Category: Medagli, B.]]	+	[[Category: Gorlach, M]]
-	[[Category: Ohlenschlager, O.]]	+	[[Category: Medagli, B]]
-	[[Category: Onesti, S.]]	+	[[Category: Ohlenschlager, O]]
-	[[Category: Wiedemann, C.]]	+	[[Category: Onesti, S]]
		+	[[Category: Wiedemann, C]]
	[[Category: Dna helicase]]		[[Category: Dna helicase]]
	[[Category: Helix-turn-helix]]		[[Category: Helix-turn-helix]]

OCA at 07:41, 29 January 2014

2014-01-29T07:41:47Z

←Older revision		Revision as of 07:41, 29 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_2m45\| PDB=2m45 \| SCENE= }}
		+	===NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus===

-	The ~~entry 2m45~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref>

-	~~Authors: Wiedemann, C~~.~~, Ohlenschlager, O~~.~~, Medagli, B~~.~~, Onesti, S~~.~~, Gorlach, M~~.	+	==About this Structure==
		+	[[2m45]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA].

-	~~Description~~: ~~NMR solution structure of the~~ C-~~terminus of the minichromosome~~ maintenance protein ~~MCM from Sulfolobus solfataricus~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: DNA helicase]]
		+	[[Category: Gorlach, M.]]
		+	[[Category: Medagli, B.]]
		+	[[Category: Ohlenschlager, O.]]
		+	[[Category: Onesti, S.]]
		+	[[Category: Wiedemann, C.]]
		+	[[Category: Dna helicase]]
		+	[[Category: Helix-turn-helix]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mcm]]
		+	[[Category: Minichromosome maintenance protein]]
		+	[[Category: Pre-replicative complex]]
		+	[[Category: Replication]]
		+	[[Category: Thermophile protein]]
		+	[[Category: Winged helix]]
		+	[[Category: Winged helix turn]]

OCA at 09:48, 13 February 2013

2013-02-13T09:48:20Z

←Older revision		Revision as of 09:48, 13 February 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2m45 is ON HOLD	+	The entry 2m45 is ON HOLD until Paper Publication

-	Authors: ~~Ohlenschlager~~, O., ~~Gorlach~~, ~~M., Wiedemann, C~~., Medagli, B., Onesti, S.	+	Authors: Wiedemann, C., Ohlenschlager, O., Medagli, B., Onesti, S., Gorlach, M.

-	Description: ~~Backbone 1H, 13C, and 15N Chemical Shift Assignments for~~ the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus	+	Description: NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus

OCA: Protected "2m45" [edit=sysop:move=sysop]

2013-02-06T12:10:21Z

Protected "2m45" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:10, 6 February 2013

OCA: New page: '''Unreleased structure''' The entry 2m45 is ON HOLD Authors: Ohlenschlager, O., Gorlach, M., Wiedemann, C., Medagli, B., Onesti, S. Description: Backbone 1H, 13C, and 15N Chemical Shi...

2013-02-06T12:10:20Z

New page: '''Unreleased structure''' The entry 2m45 is ON HOLD Authors: Ohlenschlager, O., Gorlach, M., Wiedemann, C., Medagli, B., Onesti, S. Description: Backbone 1H, 13C, and 15N Chemical Shi...

New page

'''Unreleased structure'''

The entry 2m45 is ON HOLD

Authors: Ohlenschlager, O., Gorlach, M., Wiedemann, C., Medagli, B., Onesti, S.

Description: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus