Molecular dynamics simulations of YbbAP suggest the periplasmic-side pocket is a lipid-binding site.

(A) Simulation setup. (B) 2D histogram (bins: 30 × 30) of LysoPG phosphate head group residency in the membrane upper leaflet over 15 μs coarse-grain simulation repeats of YbbAP in its apo and nucleotide-bound states. Scale is normalized to the global m...

Full description

Saved in:

Bibliographic Details
Main Author:	Martin B. L. McAndrew (22683641) (author)
Other Authors:	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)
Published:	2025
Subjects:	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
Tags:	Add Tag No Tags, Be the first to tag this record!

Be the first to leave a comment!

Molecular dynamics simulations of YbbAP suggest the periplasmic-side pocket is a lipid-binding site.

Similar Items