4pof: Difference between revisions
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==PfMCM N-terminal domain without DNA== | |||
=== | <StructureSection load='4pof' size='340' side='right' caption='[[4pof]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pof]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4POF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4POF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[4pog|4pog]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cdc21, PF0482 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=4pof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pof RCSB], [http://www.ebi.ac.uk/pdbsum/4pof PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ring-shaped MCM helicase is essential to all phases of DNA replication. The complex loads at replication origins as an inactive double-hexamer encircling duplex DNA. Helicase activation converts this species to two active single hexamers that encircle single-stranded DNA (ssDNA). The molecular details of MCM DNA interactions during these events are unknown. We determined the crystal structure of the Pyrococcus furiosus MCM N-terminal domain hexamer bound to ssDNA and define a conserved MCM-ssDNA binding motif (MSSB). Intriguingly, ssDNA binds the MCM ring interior perpendicular to the central channel with defined polarity. In eukaryotes, the MSSB is conserved in several Mcm2-7 subunits, and MSSB mutant combinations in S. cerevisiae Mcm2-7 are not viable. Mutant Mcm2-7 complexes assemble and are recruited to replication origins, but are defective in helicase loading and activation. Our findings identify an important MCM-ssDNA interaction and suggest it functions during helicase activation to select the strand for translocation. DOI: http://dx.doi.org/10.7554/eLife.01993.001. | |||
A conserved MCM single-stranded DNA binding element is essential for replication initiation.,Froelich CA, Kang S, Epling LB, Bell SP, Enemark EJ Elife. 2014 Apr 1;3:e01993. doi: 10.7554/eLife.01993. PMID:24692448<ref>PMID:24692448</ref> | |||
[[Category: Bell, S P | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Enemark, E J | </div> | ||
[[Category: Epling, L B | == References == | ||
[[Category: Froelich, C A | <references/> | ||
[[Category: Kang, S | __TOC__ | ||
</StructureSection> | |||
[[Category: Pyrfu]] | |||
[[Category: Bell, S P]] | |||
[[Category: Enemark, E J]] | |||
[[Category: Epling, L B]] | |||
[[Category: Froelich, C A]] | |||
[[Category: Kang, S]] | |||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Dna replication]] | [[Category: Dna replication]] | ||
[[Category: Ob-fold]] | [[Category: Ob-fold]] | ||
[[Category: Replication]] | [[Category: Replication]] | ||
Revision as of 13:56, 24 December 2014
PfMCM N-terminal domain without DNAPfMCM N-terminal domain without DNA
Structural highlights
Publication Abstract from PubMedThe ring-shaped MCM helicase is essential to all phases of DNA replication. The complex loads at replication origins as an inactive double-hexamer encircling duplex DNA. Helicase activation converts this species to two active single hexamers that encircle single-stranded DNA (ssDNA). The molecular details of MCM DNA interactions during these events are unknown. We determined the crystal structure of the Pyrococcus furiosus MCM N-terminal domain hexamer bound to ssDNA and define a conserved MCM-ssDNA binding motif (MSSB). Intriguingly, ssDNA binds the MCM ring interior perpendicular to the central channel with defined polarity. In eukaryotes, the MSSB is conserved in several Mcm2-7 subunits, and MSSB mutant combinations in S. cerevisiae Mcm2-7 are not viable. Mutant Mcm2-7 complexes assemble and are recruited to replication origins, but are defective in helicase loading and activation. Our findings identify an important MCM-ssDNA interaction and suggest it functions during helicase activation to select the strand for translocation. DOI: http://dx.doi.org/10.7554/eLife.01993.001. A conserved MCM single-stranded DNA binding element is essential for replication initiation.,Froelich CA, Kang S, Epling LB, Bell SP, Enemark EJ Elife. 2014 Apr 1;3:e01993. doi: 10.7554/eLife.01993. PMID:24692448[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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