2ma3

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'''Unreleased structure'''
 
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The entry 2ma3 is ON HOLD
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==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus==
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<StructureSection load='2ma3' size='340' side='right'caption='[[2ma3]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ma3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MA3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ma3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma3 OCA], [https://pdbe.org/2ma3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ma3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ma3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ma3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O27798_METTH O27798_METTH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Wiedemann, C., Ohlenschlager, O., Medagli, B., Onesti, S., Gorlach, M.
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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>
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Description: 1H, 13C, and 15N Chemical Shift Assignments for the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ma3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Methanothermobacter thermautotrophicus]]
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[[Category: Gorlach M]]
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[[Category: Medagli B]]
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[[Category: Ohlenschlager O]]
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[[Category: Onesti S]]
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[[Category: Wiedemann C]]

Current revision

NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus

PDB ID 2ma3

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