View source for 5xf8


==Cryo-EM structure of the Cdt1-MCM2-7 complex in AMPPNP state==
<SX load='5xf8' size='340' side='right' viewer='molstar' caption='[[5xf8]], [[Resolution|resolution]] 7.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xf8]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XF8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.1&#8491;</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=5xf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xf8 OCA], [https://pdbe.org/5xf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xf8 RCSB], [https://www.ebi.ac.uk/pdbsum/5xf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xf8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MCM6_YEAST MCM6_YEAST] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 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 six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The minichromosome maintenance complex (MCM) hexameric complex (Mcm2-7) forms the core of the eukaryotic replicative helicase. During G1 phase, two Cdt1-Mcm2-7 heptamers are loaded onto each replication origin by the origin-recognition complex (ORC) and Cdc6 to form an inactive MCM double hexamer (DH), but the detailed loading mechanism remains unclear. Here we examine the structures of the yeast MCM hexamer and Cdt1-MCM heptamer from Saccharomyces cerevisiae. Both complexes form left-handed coil structures with a 10-15-A gap between Mcm5 and Mcm2, and a central channel that is occluded by the C-terminal domain winged-helix motif of Mcm5. Cdt1 wraps around the N-terminal regions of Mcm2, Mcm6 and Mcm4 to stabilize the whole complex. The intrinsic coiled structures of the precursors provide insights into the DH formation, and suggest a spring-action model for the MCM during the initial origin melting and the subsequent DNA unwinding.

Open-ringed structure of the Cdt1-Mcm2-7 complex as a precursor of the MCM double hexamer.,Zhai Y, Cheng E, Wu H, Li N, Yung PY, Gao N, Tye BK Nat Struct Mol Biol. 2017 Mar;24(3):300-308. doi: 10.1038/nsmb.3374. Epub 2017, Feb 13. PMID:28191894<ref>PMID:28191894</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xf8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Cheng E]]
[[Category: Gao N]]
[[Category: Li N]]
[[Category: Tye BK]]
[[Category: Wu H]]
[[Category: Yung PY]]
[[Category: Zhai Y]]