Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins

Guilvout, Ingrid and Chami, Mohamed and Disconzi, Elena and Bayan, Nicolas and Pugsley, Anthony P. and Huysmans, Gerard H. M.. (2014) Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structure, 22 (4). pp. 582-589.

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Official URL: https://edoc.unibas.ch/87944/

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The outer membrane portal of the Klebsiella oxytoca type II secretion system, PulD, is a prototype of a family of proteins, the secretins, which are essential components of many bacterial secretion and pilus assembly machines. PulD is a homododecamer with a periplasmic vestibule and an outer chamber on either side of a membrane-spanning region that is poorly resolved by electron microscopy. Membrane insertion involves the formation of a dodecameric membrane-embedded intermediate. Here, we describe an amino acid substitution in PulD that blocks its assembly at this intermediate "prepore" stage. Electron microscopy indicated that the prepore has an apparently normal periplasmic vestibule but a poorly organized outer chamber. A peptide loop around this amino acid appears to be important for the formation/stability of the fully folded complex. A similar assembly intermediate results from creation of the same amino acid substitution in the Pseudomonas aeruginosa secretin XcpQ.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:09 Mar 2022 10:42
Deposited On:09 Mar 2022 10:42

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