4ywk

Pyrococcus furiosus MCM N-terminal domain with Zinc-binding subdomain B deleted

spinqualitylabelsall models 4ywk, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ywk is a 2 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8U3I4_PYRFU Publication Abstract from PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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