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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Détails bibliographiques
Auteur principal:	Martin B. L. McAndrew (22683641) (author)
Autres auteurs:	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)
Publié:	2025
Sujets:	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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