2V1U

STRUCTURE OF THE AEROPYRUM PERNIX ORC1 PROTEIN IN COMPLEX WITH DNA

Summary for 2V1U

• Entry DOI: 10.2210/pdb2v1u/pdb
• Descriptor: CELL DIVISION CONTROL PROTEIN 6 HOMOLOG, 5'-D(*TP*CP*TP*CP*CP*AP*CP*AP*GP*GP *AP*AP*AP*CP*GP*GP*AP*GP*GP*GP*GP*T)-3', 5'-D(*AP*CP*CP*CP*CP*TP*CP*CP*GP*TP *TP*TP*CP*CP*TP*GP*TP*GP*GP*AP*GP*A)-3', ... (6 entities in total)
• Functional Keywords: dna replication, nucleotide-binding, replication, archaea, atp-binding, phosphorylation, dna replication initiation
• Biological source: AEROPYRUM PERNIX; More
• Total number of polymer chains: 3
• Total formula weight: 57458.54

Authors

Gaudier, M.,Schuwirth, B.S.,Westcott, S.L.,Wigley, D.B. (deposition date: 2007-05-30, release date: 2007-09-18, Last modification date: 2024-05-08)

Primary citation

Gaudier, M.,Schuwirth, B.S.,Westcott, S.L.,Wigley, D.B.
Structural Basis of DNA Replication Origin Recognition by an Orc Protein.
Science, 317:1213-, 2007

PubMed Abstract: DNA replication in archaea and in eukaryotes share many similarities. We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins. DNA binding is mediated principally by a C-terminal winged helix domain that inserts deeply into the major and minor grooves, widening them both. However, additional DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a characteristic G-rich sequence, inducing a 35 degrees bend in the duplex and providing directionality to the binding site. Both contact regions also induce substantial unwinding of the DNA. The structure provides insight into the initial step in assembly of a replication origin and recruitment of minichromosome maintenance (MCM) helicase to that origin.

PubMed: 17761880
DOI: 10.1126/SCIENCE.1143664

Experimental method

X-RAY DIFFRACTION (3.1 Å)