9EFE image
Deposition Date 2024-11-20
Release Date 2025-06-11
Last Version Date 2025-06-11
Entry Detail
PDB ID:
9EFE
Title:
Crystal Structure in space group P21 of a nucleoid-associated protein (UBP) from Sulfolobus islandicus.
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.59 Å
R-Value Free:
0.25
R-Value Work:
0.22
R-Value Observed:
0.22
Space Group:
P 1 21 1
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Plasmid pARN4
Gene (Uniprot):SiRe_1573
Chain IDs:A, B (auth: C), C (auth: D), D (auth: B), E, F, G, H
Chain Length:112
Number of Molecules:8
Biological Source:Sulfolobus islandicus REY15A
Primary Citation
An archaeal nucleoid-associated protein binds an essential motif in DNA replication origins.
Nat Commun 16 5230 5230 (2025)
PMID: 40473630 DOI: 10.1038/s41467-025-60618-3

Abstact

DNA replication typically has defined start sites, or replication origins, which are designated by their recognition by specific initiator proteins. In addition to initiators, general chromatin or nucleoid-associated proteins have been shown to play roles in modulating origin efficiency in eukaryotes and bacteria. The role of chromatin proteins in origin function in the archaeal domain of life is poorly understood. Here, we describe a dissection of sequences elements required for in vivo function of an archaeal DNA replication origin. Our data reveal a hitherto uncharacterized sequence element, the ucm, is required for origin activity. We identify a protein, UBP, that interacts with the ucm and additionally with hundreds of other sites on the genome. We solve the crystal structure of UBP alone and in complex with ucm DNA, and further show that UBP interacts with the MCM replicative helicase. Taken together, our data provide evidence that UBP functions as a general nucleoid-associated protein that plays a key role in facilitating the egress of the MCM replicative helicase from DNA replication origins.

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