4ywl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ywl]] is a 10 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=4YWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWL FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ywl]] is a 10 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=4YWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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]] 3.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=4ywl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywl OCA], [https://pdbe.org/4ywl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ywl RCSB], [https://www.ebi.ac.uk/pdbsum/4ywl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywl 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=4ywl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywl OCA], [https://pdbe.org/4ywl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ywl RCSB], [https://www.ebi.ac.uk/pdbsum/4ywl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:08, 27 September 2023
Pyrococcus furiosus MCM N-terminal domain F179A point mutant pentameric ringPyrococcus furiosus MCM N-terminal domain F179A point mutant pentameric ring
Structural highlights
FunctionPublication Abstract from PubMedThe hexameric Minichromosome Maintenance (MCM) protein complex forms a ring that unwinds DNA at the replication fork in eukaryotes and archaea. Our recent crystal structure of an archaeal MCM N-terminal domain bound to single-stranded DNA (ssDNA) revealed ssDNA associating across tight subunit interfaces but not at the loose interfaces, indicating that DNA-binding is governed not only by the DNA-binding residues of the subunits (MCM ssDNA-binding motif, MSSB) but also by the relative orientation of the subunits. We now extend these findings by showing that DNA-binding by the MCM N-terminal domain of the archaeal organism Pyrococcus furiosus occurs specifically in the hexameric oligomeric form. We show that mutants defective for hexamerization are defective in binding ssDNA despite retaining all the residues observed to interact with ssDNA in the crystal structure. One mutation that exhibits severely defective hexamerization and ssDNA-binding is at a conserved phenylalanine that aligns with the mouse Mcm4(Chaos3) mutation associated with chromosomal instability, cancer, and decreased intersubunit association. MCM ring hexamerization is a prerequisite for DNA-binding.,Froelich CA, Nourse A, Enemark EJ Nucleic Acids Res. 2015 Sep 13. pii: gkv914. PMID:26365238[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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