3fxe

Crystal structure of interacting domains of IcmR and IcmQ (seleno-derivative)

spinqualitylabelsall models 3fxe, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fxe is a 2 chain structure with sequence from Legpc and Legph. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: icmQ, LPC_2899 (LEGPC), icmR, lpg0443 (LEGPH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila.,Raychaudhury S, Farelli JD, Montminy TP, Matthews M, Menetret JF, Dumenil G, Roy CR, Head JF, Isberg RR, Akey CW Structure. 2009 Apr 15;17(4):590-601. PMID:19368892 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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