6f0l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "6f0l" [edit=sysop:move=sysop])
Current revision (05:12, 21 November 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6f0l is ON HOLD
+
==S. cerevisiae MCM double hexamer bound to duplex DNA==
 +
<SX load='6f0l' size='340' side='right' viewer='molstar' caption='[[6f0l]], [[Resolution|resolution]] 4.77&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[6f0l]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F0L 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]] 4.77&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=6f0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0l OCA], [https://pdbe.org/6f0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f0l RCSB], [https://www.ebi.ac.uk/pdbsum/6f0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0l ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MCM2_YEAST MCM2_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; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Eukaryotic origins of replication are licensed upon loading of the MCM helicase motor onto DNA. ATP hydrolysis by MCM is required for loading and the post-catalytic MCM is an inactive double hexamer that encircles duplex DNA. Origin firing depends on MCM engagement of Cdc45 and GINS to form the CMG holo-helicase. CMG assembly requires several steps including MCM phosphorylation by DDK. To understand origin activation, here we have determined the cryo-EM structures of DNA-bound MCM, either unmodified or phosphorylated, and visualize a phospho-dependent MCM element likely important for Cdc45 recruitment. MCM pore loops touch both the Watson and Crick strands, constraining duplex DNA in a bent configuration. By comparing our new MCM-DNA structure with the structure of CMG-DNA, we suggest how the conformational transition from the loaded, post-catalytic MCM to CMG might promote DNA untwisting and melting at the onset of replication.
-
Authors: Abid Ali, F., Pye, V.E., Douglas, M.E., Locke, J., Nans, A., Diffley, J.F.X., Costa, A.
+
Cryo-EM structure of a licensed DNA replication origin.,Abid Ali F, Douglas ME, Locke J, Pye VE, Nans A, Diffley JFX, Costa A Nat Commun. 2017 Dec 21;8(1):2241. doi: 10.1038/s41467-017-02389-0. PMID:29269875<ref>PMID:29269875</ref>
-
Description: S. cerevisiae MCM double hexamer bound to duplex DNA
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Nans, A]]
+
<div class="pdbe-citations 6f0l" style="background-color:#fffaf0;"></div>
-
[[Category: Pye, V.E]]
+
== References ==
-
[[Category: Abid Ali, F]]
+
<references/>
-
[[Category: Douglas, M.E]]
+
__TOC__
-
[[Category: Diffley, J.F.X]]
+
</SX>
-
[[Category: Locke, J]]
+
[[Category: Large Structures]]
-
[[Category: Costa, A]]
+
[[Category: Saccharomyces cerevisiae S288C]]
 +
[[Category: Synthetic construct]]
 +
[[Category: Abid Ali F]]
 +
[[Category: Costa A]]
 +
[[Category: Diffley JFX]]
 +
[[Category: Douglas ME]]
 +
[[Category: Locke J]]
 +
[[Category: Nans A]]
 +
[[Category: Pye VE]]

Current revision

S. cerevisiae MCM double hexamer bound to duplex DNA

6f0l, resolution 4.77Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6f0l"
Personal tools