6wgf: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==Atomic model of mutant Mcm2-7 hexamer with Mcm6 WHD truncation== | ||
<StructureSection load='6wgf' size='340' side='right'caption='[[6wgf]]' scene=''> | <StructureSection load='6wgf' size='340' side='right'caption='[[6wgf]], [[Resolution|resolution]] 7.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6wgf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WGF FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.7Å</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=6wgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wgf OCA], [https://pdbe.org/6wgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wgf RCSB], [https://www.ebi.ac.uk/pdbsum/6wgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wgf ProSAT]</span></td></tr> | |||
</table> | </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> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Z | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bai L]] | |||
[[Category: Dodd T]] | |||
[[Category: Ivanov I]] | |||
[[Category: Li H]] | |||
[[Category: Magdalou I]] | |||
[[Category: Riera A]] | |||
[[Category: Schneider S]] | |||
[[Category: Speck C]] | |||
[[Category: Stillman B]] | |||
[[Category: Yan C]] | |||
[[Category: Yuan Z]] | |||
Latest revision as of 17:44, 6 March 2024
Atomic model of mutant Mcm2-7 hexamer with Mcm6 WHD truncationAtomic model of mutant Mcm2-7 hexamer with Mcm6 WHD truncation
Structural highlights
FunctionMCM2_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.[1] [2] References
|
| ||||||||||||||||