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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 [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/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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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'>[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='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 ==
== 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_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;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m45" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA helicase]]
[[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]]

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