4r7y: Difference between revisions
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''' | ==Crystal structure of an active MCM hexamer== | ||
<StructureSection load='4r7y' size='340' side='right' caption='[[4r7y]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r7y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R7Y FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r7z|4r7z]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r7y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r7y RCSB], [http://www.ebi.ac.uk/pdbsum/4r7y PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In a previous Research article (<xref>Froelich et al., 2014</xref>), we suggested an MCM helicase activation mechanism, but were limited in discussing the ATPase domain because it was absent from the crystal structure. Here we present the crystal structure of a nearly full-length MCM hexamer that is helicase-active and thus has all features essential for unwinding DNA. The structure is a chimera of Sulfolobus solfataricus N-terminal domain and Pyrococcus furiosus ATPase domain. We discuss three major findings: 1) a novel conformation for the A-subdomain that could play a role in MCM regulation; 2) interaction of a universally conserved glutamine in the N-terminal Allosteric Communication Loop with the AAA+ domain helix-2-insert (h2i); and 3) a recessed binding pocket for the MCM ssDNA-binding motif influenced by the h2i. We suggest that during helicase activation, the h2i clamps down on the leading strand to facilitate strand retention and regulate ATP hydrolysis. | |||
Analysis of the crystal structure of an active MCM hexamer.,Miller JM, Arachea BT, Epling LB, Enemark EJ Elife. 2014 Sep 29;3. doi: 10.7554/eLife.03433. PMID:25262915<ref>PMID:25262915</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA helicase]] | |||
[[Category: Arachea, B T.]] | |||
[[Category: Enemark, E J.]] | |||
[[Category: Epling, L B.]] | |||
[[Category: Miller, J M.]] | |||
[[Category: Aaa+]] | |||
[[Category: Atpase]] | |||
[[Category: Dna replication]] | |||
[[Category: Helicase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mcm]] | |||
[[Category: Ob-fold]] | |||
Revision as of 07:43, 8 October 2014
Crystal structure of an active MCM hexamer
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