Binding and unwinding: SF3 viral helicases.

Full Abstract

The SF3 helicases, distinct from the more prevalent SF1 and SF2 helicases, were originally identified in the genomes of small DNA and RNA viruses. The first crystal structures of SF3 helicases have been determined, revealing a closer structural relationship to AAA+ proteins than to RecA, consistent with their participation in replication initiation. In conjunction with origin-binding domains, SF3 helicases are responsible for distorting DNA before replication forks can be assembled. At these forks, the SF3 helicases act as replicative helicases. The simian virus 40 SF3 helicase forms a hexameric ring, anticipated to be characteristic of the entire superfamily.

Author information

Author/s: Hickman, Alison Burgess (AB); Dyda, Fred (F);

Affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 5 Center Drive MSC 0560, Bethesda, MD 20892-0560, USA.

Journal and publication information

Publication Type: Journal Article; Review

Journal: Current opinion in structural biology (Curr Opin Struct Biol), published in England. (Language: eng)

Reference: 2005-Feb; vol 15 (issue 1) : pp 77-85

Dates: Created 2005/02/18; Completed 2005/06/24; Revised 2006/11/15;

PMID: 15718137, status: MEDLINE (last retrieved date: 2/18/2009)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

External Links for this article
(including full text providers, if available):

Click Electronic Full-text Provider Links to see options for finding the electronic full text links to this article. Note there may be a subscription or fee required for access to the full text. See our FAQ for information on finding FREE full text articles.

This article may also be located in paper journal collections available in many libraries. Use the Journal and Publication Information above to find the full article.