2m45: Difference between revisions

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-{{STRUCTURE_2m45|  PDB=2m45  |  SCENE=  }}
-===NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus===
-==Function==
+==NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus==
-[[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>
+<StructureSection load='2m45' size='340' side='right'caption='[[2m45]]' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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>
+== Function ==
+[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.
-==About this Structure==
+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>
-[[2m45]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M45 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<references group="xtra"/><references/>
+</div>
-[[Category: DNA helicase]]
+<div class="pdbe-citations 2m45" style="background-color:#fffaf0;"></div>
-[[Category: Gorlach, M.]]
+== References ==
-[[Category: Medagli, B.]]
+<references/>
-[[Category: Ohlenschlager, O.]]
+__TOC__
-[[Category: Onesti, S.]]
+</StructureSection>
-[[Category: Wiedemann, C.]]
+[[Category: Large Structures]]
-[[Category: Dna helicase]]
+[[Category: Saccharolobus solfataricus P2]]
-[[Category: Helix-turn-helix]]
+[[Category: Gorlach M]]
-[[Category: Hydrolase]]
+[[Category: Medagli B]]
-[[Category: Mcm]]
+[[Category: Ohlenschlager O]]
-[[Category: Minichromosome maintenance protein]]
+[[Category: Onesti S]]
-[[Category: Pre-replicative complex]]
+[[Category: Wiedemann C]]
-[[Category: Replication]]
-[[Category: Thermophile protein]]
-[[Category: Winged helix]]
-[[Category: Winged helix turn]]