AI Article Synopsis
- The integral membrane enzyme PagP helps E. coli evade immune responses by transferring a palmitoyl group from a phospholipid to lipid A.
- PagP features an internal hydrocarbon ruler within its β barrel structure, which measures the palmitoyl group during the transfer.
- Studies using molecular dynamics and crystal structure analysis reveal that the phospholipid enters PagP through a specific gap, allowing the head group to stay outside while the hydrophobic tail moves into the protein.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5007126 | PMC |
| http://dx.doi.org/10.1016/j.str.2010.06.014 | DOI Listing |
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