4pof: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pof]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4POF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pof]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4POF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.648Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4pof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pof OCA], [https://pdbe.org/4pof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pof RCSB], [https://www.ebi.ac.uk/pdbsum/4pof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pof ProSAT]</span></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=4pof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pof OCA], [https://pdbe.org/4pof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pof RCSB], [https://www.ebi.ac.uk/pdbsum/4pof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pof ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 20:19, 20 September 2023
PfMCM N-terminal domain without DNAPfMCM N-terminal domain without DNA
Structural highlights
FunctionPublication 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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