3jqo

Crystal structure of the outer membrane complex of a type IV secretion system

spinqualitylabelsall models 3jqo, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jqo is a 42 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: LDA, MPD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q46705_ECOLX 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 Type IV secretion systems are secretion nanomachines spanning the two membranes of Gram-negative bacteria. Three proteins, VirB7, VirB9 and VirB10, assemble into a 1.05 megadalton (MDa) core spanning the inner and outer membranes. This core consists of 14 copies of each of the proteins and forms two layers, the I and O layers, inserting in the inner and outer membrane, respectively. Here we present the crystal structure of a approximately 0.6 MDa outer-membrane complex containing the entire O layer. This structure is the largest determined for an outer-membrane channel and is unprecedented in being composed of three proteins. Unexpectedly, this structure identifies VirB10 as the outer-membrane channel with a unique hydrophobic double-helical transmembrane region. This structure establishes VirB10 as the only known protein crossing both membranes of Gram-negative bacteria. Comparison of the cryo-electron microscopy (cryo-EM) and crystallographic structures points to conformational changes regulating channel opening and closing. Structure of the outer membrane complex of a type IV secretion system.,Chandran V, Fronzes R, Duquerroy S, Cronin N, Navaza J, Waksman G Nature. 2009 Dec 24;462(7276):1011-5. Epub 2009 Nov 29. PMID:19946264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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