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A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase

DOI: 10.1016/j.febslet.2010.09.006 DOI Help

Authors: Arefeh Seyedarabi (Queen Mary University of London) , James A. Sullivan (Queen Mary University of London) , Chihiro Sasakawa (University of Tokyo) , Richard W. Pickersgill (Queen Mary University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: September 2010

Abstract: We show that the monomeric form of Shigella IpaH9.8 E3 ligase catalyses the ubiquitination of human U2AF35 in vitro, providing a molecular mechanism for the observed in vivo effect. We further discover that under non-reducing conditions IpaH9.8 undergoes a domain swap driven by the formation of a disulfide bridge involving the catalytic cysteine and that this dimer is unable to catalyse the ubiquitination of U2AF35. The crystal structure of the domain-swapped dimer is presented. The redox inactivation of IpaH9.8 could be a mechanism of regulating the activity of the IpaH9.8 E3 ligase in response to cell damage so that the host cell in which the bacteria resides is maintained in a benign state suitable for bacterial survival.

Journal Keywords: Ipah9.8; E3 Ubiquitin Ligase; Domain Swap; U2Af35; Shigella Flexneri

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 23/09/2010 14:06

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)