2ma3: Difference between revisions

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New page: '''Unreleased structure''' The entry 2ma3 is ON HOLD Authors: Wiedemann, C., Ohlenschlager, O., Medagli, B., Onesti, S., Gorlach, M. Description: 1H, 13C, and 15N Chemical Shift Assign...
 
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'''Unreleased structure'''


The entry 2ma3 is ON HOLD
==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]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O27798_METTH O27798_METTH]
<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.


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


Description: 1H, 13C, and 15N Chemical Shift Assignments for the C-terminus of the minichromosome maintenance protein MCM from Methanothermobacter thermautotrophicus
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ma3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Gorlach M]]
[[Category: Medagli B]]
[[Category: Ohlenschlager O]]
[[Category: Onesti S]]
[[Category: Wiedemann C]]