1KSY

Crystal Structures of Two Intermediates in the Assembly of the Papillomavirus Replication Initiation Complex

Summary for 1KSY

• Entry DOI: 10.2210/pdb1ksy/pdb
• Related: 1F08 1KSX
• Descriptor: E1 Recognition Sequence, Strand 1, E1 Recognition Sequence, Strand 2, REPLICATION PROTEIN E1, ... (4 entities in total)
• Functional Keywords: papillomavirus, dna-binding domain, replication, initiator protein, helicase, replication-dna complex, replication/dna
• Biological source: Bovine papillomavirus
• Cellular location: Host nucleus: P03116
• Total number of polymer chains: 6
• Total formula weight: 72011.04

Authors

Enemark, E.J.,Stenlund, A.,Joshua-Tor, L. (deposition date: 2002-01-14, release date: 2002-03-15, Last modification date: 2023-08-16)

Primary citation

Enemark, E.J.,Stenlund, A.,Joshua-Tor, L.
Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.
EMBO J., 21:1487-1496, 2002

PubMed Abstract: Initiation of DNA replication of the papillomavirus genome is a multi-step process involving the sequential loading of viral E1 protein subunits onto the origin of replication. Here we have captured structural snapshots of two sequential steps in the assembly process. Initially, an E1 dimer binds to adjacent major grooves on one face of the double helix; a second dimer then binds to another face of the helix. Each E1 monomer has two DNA-binding modules: a DNA-binding loop, which binds to one DNA strand and a DNA-binding helix, which binds to the opposite strand. The nature of DNA binding suggests a mechanism for the transition between double- and single-stranded DNA binding that is implicit in the progression to a functional helicase.

PubMed: 11889054
DOI: 10.1093/emboj/21.6.1487

Experimental method

X-RAY DIFFRACTION (3.05 Å)