5ZR1
Saccharomyces Cerevisiae Origin Recognition Complex Bound to a 72-bp Origin DNA containing ACS and B1 element
Summary for 5ZR1
Entry DOI | 10.2210/pdb5zr1/pdb |
EMDB information | 6941 6942 6943 |
Descriptor | Origin recognition complex subunit 1, MAGNESIUM ION, Origin recognition complex subunit 2, ... (10 entities in total) |
Functional Keywords | origin recognition complex, dna replication initiation, 72-bp origin dna, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 8 |
Total formula weight | 460559.30 |
Authors | |
Primary citation | Li, N.,Lam, W.H.,Zhai, Y.,Cheng, J.,Cheng, E.,Zhao, Y.,Gao, N.,Tye, B.K. Structure of the origin recognition complex bound to DNA replication origin. Nature, 559:217-222, 2018 Cited by PubMed Abstract: The six-subunit origin recognition complex (ORC) binds to DNA to mark the site for the initiation of replication in eukaryotes. Here we report a 3 Å cryo-electron microscopy structure of the Saccharomyces cerevisiae ORC bound to a 72-base-pair origin DNA sequence that contains the ARS consensus sequence (ACS) and the B1 element. The ORC encircles DNA through extensive interactions with both phosphate backbone and bases, and bends DNA at the ACS and B1 sites. Specific recognition of thymine residues in the ACS is carried out by a conserved basic amino acid motif of Orc1 in the minor groove, and by a species-specific helical insertion motif of Orc4 in the major groove. Moreover, similar insertions into major and minor grooves are also embedded in the B1 site by basic patch motifs from Orc2 and Orc5, respectively, to contact bases and to bend DNA. This work pinpoints a conserved role of ORC in modulating DNA structure to facilitate origin selection and helicase loading in eukaryotes. PubMed: 29973722DOI: 10.1038/s41586-018-0293-x PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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