Javascript must be enabled for the correct page display

S-component interactions with group I and II ECF transport mechanisms and how they are mediated

Thai, Moudon (2022) S-component interactions with group I and II ECF transport mechanisms and how they are mediated. Bachelor's Thesis, Biology.

[img]
Preview
Text
bBIO_2022_ThaiM.pdf

Download (646kB) | Preview
[img] Text
Toestemming.pdf
Restricted to Registered users only

Download (125kB)

Abstract

The ECF transporter is a subgroup within the ABC transporter family which could serve as a new potential antibiotic target as the ECF transporter is prevalent in numerous human pathogens. The ECF transporter consists of two ATPases, an S-component which is specifically coded for a substrate and the T-component to which the S-component is bound to. The scope of the thesis is to describe the mechanism of the S-component with the ECF transport mechanism. Findings show that in group I ECF transporters, the S-component binds with the substrate upon ATP binding. Due to ATP hydrolysis, the coupling helices of the T component change its conformation causing the S-component to topple over (in which the S-component will be parallel to the membrane) and release the substrate into the cell. In group II ECF transporters ATP binding causes the S-component to be released from the ECF complex and bind to its substrate in the free environment. Toppling happens in the free environment which is membrane-mediated, however, this has not been tested in vitro. Then the S-component binds to the ECF complex with their complementary hydrophobic surfaces and the substrate is then released into the cell. These findings create a better understanding of the ECF transport mechanism and future research could provide more insight into this and ultimately create potential antibiotic targets against the ECF transporter.

Item Type: Thesis (Bachelor's Thesis)
Supervisor name: Scheffers, D.J.
Degree programme: Biology
Thesis type: Bachelor's Thesis
Language: English
Date Deposited: 26 Jul 2022 07:23
Last Modified: 26 Jul 2022 07:23
URI: https://fse.studenttheses.ub.rug.nl/id/eprint/28149

Actions (login required)

View Item View Item