4a5p

Structure of the Shigella flexneri MxiA protein

spinqualitylabelsall models 4a5p, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a5p is a 3 chain structure with sequence from Shigella flexneri 5a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO NonStd Res: MLY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MXIA_SHIFL] Necessary for the secretion of IPA invasins. Publication Abstract from PubMed Type III secretion systems (T3SSs) are bacterial membrane-embedded nanomachines designed to export specifically targeted proteins from the bacterial cytoplasm. Secretion through T3SS is governed by a subset of inner membrane proteins termed the 'export apparatus'. We show that a key member of the Shigella flexneri export apparatus, MxiA, assembles into a ring essential for secretion in vivo. The ring-forming interfaces are well-conserved in both nonflagellar and flagellar homologs, implying that the ring is an evolutionarily conserved feature in these systems. Electron cryo-tomography revealed a T3SS-associated cytoplasmic torus of size and shape corresponding to those of the MxiA ring aligned to the secretion channel located between the secretion pore and the ATPase complex. This defines the molecular architecture of the dominant component of the export apparatus and allows us to propose a model for the molecular mechanisms controlling secretion. Architecture of the major component of the type III secretion system export apparatus.,Abrusci P, Vergara-Irigaray M, Johnson S, Beeby MD, Hendrixson DR, Roversi P, Friede ME, Deane JE, Jensen GJ, Tang CM, Lea SM Nat Struct Mol Biol. 2013 Jan;20(1):99-104. doi: 10.1038/nsmb.2452. Epub 2012 Dec, 9. PMID:23222644 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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