3GP6

Crystal structure of PagP in SDS/MPD

Summary for 3GP6

• Entry DOI: 10.2210/pdb3gp6/pdb
• Related: 1MM4 1MM5 1THQ
• Descriptor: Protein pagP, DODECYL SULFATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (7 entities in total)
• Functional Keywords: palmitoyltransferase, beta-barrel, outer membrane enzyme, pagp, sds, mpd, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 22610.82

Authors

Cuesta-Seijo, J.A.,Prive, G.G. (deposition date: 2009-03-20, release date: 2010-06-23, Last modification date: 2023-09-06)

Primary citation

Cuesta-Seijo, J.A.,Neale, C.,Khan, M.A.,Moktar, J.,Tran, C.D.,Bishop, R.E.,Pomes, R.,Prive, G.G.
PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.
Structure, 18:1210-1219, 2010

PubMed Abstract: Enzymatic reactions involving bilayer lipids occur in an environment with strict physical and topological constraints. The integral membrane enzyme PagP transfers a palmitoyl group from a phospholipid to lipid A in order to assist Escherichia coli in evading host immune defenses during infection. PagP measures the palmitoyl group with an internal hydrocarbon ruler that is formed in the interior of the eight-stranded antiparallel β barrel. The access and egress of the palmitoyl group is thought to take a lateral route from the bilayer phase to the barrel interior. Molecular dynamics, mutagenesis, and a 1.4 A crystal structure of PagP in an SDS / 2-methyl-2,4-pentanediol (MPD) cosolvent system reveal that phospholipid access occurs at the crenel present between strands F and G of PagP. In this way, the phospholipid head group can remain exposed to the cell exterior while the lipid acyl chain remains in a predominantly hydrophobic environment as it translocates to the protein interior.

PubMed: 20826347
DOI: 10.1016/j.str.2010.06.014

Experimental method

X-RAY DIFFRACTION (1.4 Å)