2ma3
From Proteopedia
(Difference between revisions)
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| - | == | + | ==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus== |
<StructureSection load='2ma3' size='340' side='right' caption='[[2ma3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2ma3' size='340' side='right' caption='[[2ma3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</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=2ma3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ma3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ma3 PDBsum]</span></td></tr> | </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=2ma3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ma3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ma3 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <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. | ||
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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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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:30, 20 May 2015
NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus
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