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Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations.

07:00 EST 10th February 2020 | BioPortfolio

Summary of "Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations."

Escherichia coli lipoprotein precursors at the inner membrane undergo three maturation stages before transport by the Lol system to the outer membrane. Here, we develop a pipeline to simulate the membrane association of bacterial lipoproteins in their four maturation states. This has enabled us to model and simulate 81 of the predicted 114 E. coli lipoproteins and reveal their interactions with the host lipid membrane. As part of this set we characterize the membrane contacts of LolB, the lipoprotein involved in periplasmic translocation. We also consider the means and bioenergetics for lipoprotein localization. Our calculations uncover a preference for LolB over LolA and therefore indicate how a lipoprotein may be favorably transferred from the inner to outer membrane. Finally, we reveal that LolC has a role in membrane destabilization, thereby promoting lipoprotein transfer to LolA.

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This article was published in the following journal.

Name: Structure (London, England : 1993)
ISSN: 1878-4186
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Medical and Biotech [MESH] Definitions

Periplasmic proteins that scavenge or sense diverse nutrients. In the bacterial environment they usually couple to transporters or chemotaxis receptors on the inner bacterial membrane.

Gram-negative bacterial secretion systems which translocate effectors in a single step across the inner and outer membranes. The one-step secretion is carried out by a channel that passes from the CYTOPLASM, through the inner membrane, PERIPLASMIC SPACE, and outer membrane, to the EXTRACELLULAR SPACE. The specificity of type I secretions systems are determined by the specificity of the three subcomponents forming the channel - an ATP transporter (ATP-BINDING CASSETTE TRANSPORTERS); a membrane fusion protein (MEMBRANE FUSION PROTEINS); and an outer membrane protein (BACTERIAL OUTER MEMBRANE PROTEINS.)

Proteins that bind to and transfer CHOLESTEROL ESTERS between LIPOPROTEINS such as LOW-DENSITY LIPOPROTEINS and HIGH-DENSITY LIPOPROTEINS.

Gram-negative bacterial secretion systems which carry out the secretion of folded proteins.T2SSs secrete folded proteins from the PERIPLASMIC SPACE that have been exported there by SEC TRANSLOCASE or TAT SECRETION SYSTEMS, or they secrete folded proteins directly from the CYTOPLASM. The T2SSs have four substructures, an ATPase, an inner membrane platform, a pseudopilin, and secretin, an outer membrane complex which is a channel for secretion. (This bacterial secretin is not the same as the mammalian hormone also named SECRETIN.)

Conditions with abnormally low levels of LIPOPROTEINS in the blood. This may involve any of the lipoprotein subclasses, including ALPHA-LIPOPROTEINS (high-density lipoproteins); BETA-LIPOPROTEINS (low-density lipoproteins); and PREBETA-LIPOPROTEINS (very-low-density lipoproteins).

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