8ZP5
Cryo-EM structure of origin recognition complex (Orc5 basic patch mutations) with ARS1 DNA bound
Summary for 8ZP5
Entry DOI | 10.2210/pdb8zp5/pdb |
EMDB information | 60327 |
Descriptor | Origin recognition complex subunit 2, MAGNESIUM ION, Origin recognition complex subunit 5, ... (10 entities in total) |
Functional Keywords | replication |
Biological source | Saccharomyces cerevisiae S288C More |
Total number of polymer chains | 8 |
Total formula weight | 463425.84 |
Authors | |
Primary citation | Lam, W.H.,Yu, D.,Zhang, Q.,Lin, Y.,Li, N.,Li, J.,Wu, Y.,Zhang, Y.,Gao, N.,Tye, B.K.,Zhai, Y.,Dang, S. DNA bending mediated by ORC is essential for replication licensing in budding yeast. Proc.Natl.Acad.Sci.USA, 122:e2502277122-e2502277122, 2025 Cited by PubMed Abstract: In eukaryotes, the origin recognition complex (ORC) promotes the assembly of minichromosome maintenance 2 to 7 complexes into a head-to-head double hexamer at origin DNA in a process known as replication licensing. In this study, we present a series of cryoelectron microscopy structures of yeast ORC mutants in complex with origin DNA. We show that Orc6, the smallest subunit of ORC, utilizes its transcription factor II B-B domain to orchestrate the sequential binding of ORC to origin DNA. In addition, Orc6 plays the role of a scaffold by stabilizing the basic patch (BP) of Orc5 for ORC to capture and bend origin DNA. Importantly, disrupting DNA bending through mutating three key residues in Orc5-BP impairs ORC's ability to promote replication initiation at two points during the pre-RC assembly process. This study dissects the multifaceted role of Orc6 in orchestrating ORC's activities on DNA and underscores the vital role of DNA bending by ORC in replication licensing. PubMed: 40184174DOI: 10.1073/pnas.2502277122 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.98 Å) |
Structure validation
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