Identification of TesA as the periplasmic partner of YbbAP.

Identification of TesA as the periplasmic partner of YbbAP.

<p><b>(A)</b> Pairwise <i><i>in silico</i></i> co-folding of YbbP with all sec/tat secreted proteins from <i><i>Escherichia coli</i></i>. Each co-fold attempt is represented on the 2D plot by their pDockQ score and Molprobity clash sc...

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Detalles Bibliográficos
Autor principal: Martin B. L. McAndrew (22683641) (author)
Otros Autores: Jonathan Cook (3435386) (author), Amy Gill (14910614) (author), Kavya Sahoo (22683644) (author), Clare Thomas (7943747) (author), Phillip J. Stansfeld (1267617) (author), Allister Crow (263807) (author)
Publicado: 2025
Materias:
Biophysics
Biochemistry
Microbiology
Cell Biology
Molecular Biology
Biotechnology
Developmental Biology
Cancer
Hematology
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Information Systems not elsewhere classified
tolc efflux pump
multifunctional hydrolytic enzyme
extracts hydrophobic compounds
extracting hydrophobic molecules
capture implied long
bacterial cell envelope
active site residues
lipid hydrolase complex
escherichia coli </
data suggests ybbap
abc superfamily ’
div >< p
coli </
abc superfamily
thioester substrates
tesa complex
structural characterization
remarkable diversity
new function
mechanotransmission mechanism
inner membrane
extensively characterized
experimentally confirm
complete ybbap
>, three
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