3FXD

Crystal structure of interacting domains of IcmR and IcmQ

Summary for 3FXD

• Entry DOI: 10.2210/pdb3fxd/pdb
• Related: 3FXE
• Descriptor: Protein IcmQ, Protein IcmR (3 entities in total)
• Functional Keywords: 4 helix bundle, helix-turn-helix, unknown function
• Biological source: Legionella pneumophila; More
• Total number of polymer chains: 4
• Total formula weight: 28610.72

Authors

Raychaudhury, S.,Akey, C.W.,Head, J.F. (deposition date: 2009-01-20, release date: 2009-04-28, Last modification date: 2023-09-06)

Primary citation

Raychaudhury, S.,Farelli, J.D.,Montminy, T.P.,Matthews, M.,Menetret, J.F.,Dumenil, G.,Roy, C.R.,Head, J.F.,Isberg, R.R.,Akey, C.W.
Structure and Function of Interacting IcmR-IcmQ Domains from a Type IVb Secretion System in Legionella pneumophila.
Structure, 17:590-601, 2009

PubMed Abstract: During infection, Legionella pneumophila creates a replication vacuole within eukaryotic cells and this requires a Type IVb secretion system (T4bSS). IcmQ plays a critical role in the translocase and associates with IcmR. In this paper, we show that the N-terminal domain of IcmQ (Qn) mediates self-dimerization, whereas the C-terminal domain with a basic linker promotes membrane association. In addition, the binding of IcmR to IcmQ prevents self-dimerization and also blocks membrane permeabilization. However, IcmR does not completely block membrane binding by IcmQ. We then determined crystal structures of Qn with the interacting region of IcmR. In this complex, each protein forms an alpha-helical hairpin within a parallel four-helix bundle. The amphipathic nature of helices in Qn suggests two possible models for membrane permeabilization by IcmQ. The Rm-Qn structure also suggests how IcmR-like proteins in other L. pneumophila species may interact with their IcmQ partners.

PubMed: 19368892
DOI: 10.1016/j.str.2009.02.011

Experimental method

X-RAY DIFFRACTION (2.1 Å)