4A5P

Structure of the Shigella flexneri MxiA protein

Summary for 4A5P

• Entry DOI: 10.2210/pdb4a5p/pdb
• Descriptor: PROTEIN MXIA, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: protein transport, type three secretion, export apparatus, nonamer
• Biological source: SHIGELLA FLEXNERI
• Total number of polymer chains: 3
• Total formula weight: 132349.77

Authors

Abrusci, P.,Vegara-Irigaray, M.,Johnson, S.,Roversi, P.,Friede, M.E.,Deane, J.E.,Tang, C.M.,Lea, S.M. (deposition date: 2011-10-26, release date: 2012-11-14, Last modification date: 2023-12-20)

Primary citation

Abrusci, P.,Vergara-Irigaray, M.,Johnson, S.,Beeby, M.D.,Hendrixson, D.R.,Roversi, P.,Friede, M.E.,Deane, J.E.,Jensen, G.J.,Tang, C.M.,Lea, S.M.
Architecture of the major component of the type III secretion system export apparatus.
Nat.Struct.Mol.Biol., 20:99-104, 2013

PubMed Abstract: 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.

PubMed: 23222644
DOI: 10.1038/nsmb.2452

Experimental method

X-RAY DIFFRACTION (3.15 Å)