2V9P

Crystal structure of papillomavirus E1 hexameric helicase DNA-free form

Summary for 2V9P

• Entry DOI: 10.2210/pdb2v9p/pdb
• Related: 1F08 1KSX 1KSY 2GXA
• Descriptor: REPLICATION PROTEIN E1, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: aaa+ molecular motor, dna replication, dna translocation, nucleotide-binding, dna-binding, replication, early protein, atpase, nucleus, helicase, hydrolase, atp-binding
• Biological source: BOVINE PAPILLOMAVIRUS TYPE 1
• Cellular location: Host nucleus: P03116
• Total number of polymer chains: 12
• Total formula weight: 417595.50

Authors

Sanders, C.M.,Kovalevskiy, O.V.,Sizov, D.,Lebedev, A.A.,Isupov, M.N.,Antson, A.A. (deposition date: 2007-08-24, release date: 2007-10-02, Last modification date: 2023-12-13)

Primary citation

Sanders, C.M.,Kovalevskiy, O.V.,Sizov, D.,Lebedev, A.A.,Isupov, M.N.,Antson, A.A.
Papillomavirus E1 Helicase Assembly Maintains an Asymmetric State in the Absence of DNA and Nucleotide Cofactors.
Nucleic Acids Res., 35:6451-, 2007

PubMed Abstract: Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first time observed in the absence of nucleotide cofactors and DNA. Surprisingly, the ATP-binding sites adopt specific conformations linked to positional changes in the DNA-binding hairpins, which follow a wave-like trajectory, as observed previously in the E1/DNA/ADP complex. The protein's assembly thus maintains such an asymmetric state in the absence of DNA and nucleotide cofactors, allowing consideration of the E1 helicase action as the propagation of a conformational wave around the protein ring. The data imply that the wave's propagation within the AAA+ domains is not necessarily coupled with a strictly sequential hydrolysis of ATP. Since a single ATP hydrolysis event would affect the whole hexamer, such events may simply serve to rectify the direction of the wave's motion.

PubMed: 17881379
DOI: 10.1093/NAR/GKM705

Experimental method

X-RAY DIFFRACTION (3 Å)