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5ZR1

Saccharomyces Cerevisiae Origin Recognition Complex Bound to a 72-bp Origin DNA containing ACS and B1 element

Summary for 5ZR1
Entry DOI10.2210/pdb5zr1/pdb
EMDB information6941 6942 6943
DescriptorOrigin recognition complex subunit 1, MAGNESIUM ION, Origin recognition complex subunit 2, ... (10 entities in total)
Functional Keywordsorigin recognition complex, dna replication initiation, 72-bp origin dna, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
More
Total number of polymer chains8
Total formula weight460559.30
Authors
Li, N.,Lam, W.H.,Zhai, Y.,Cheng, J.,Cheng, E.,Zhao, Y.,Gao, N.,Tye, B.K. (deposition date: 2018-04-21, release date: 2018-07-11, Last modification date: 2024-03-27)
Primary citationLi, 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: 29973722
DOI: 10.1038/s41586-018-0293-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

226707

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