Poster Title

Mapping interactions between the type-VI secretion system effector Tae1 and its putative substrates using NMR spectroscopy

Research Mentor(s)

Spencer Anthony-Cahill

Affiliated Department

Chemistry

Sort Order

26

Start Date

14-5-2015 10:00 AM

End Date

14-5-2015 2:00 PM

Document Type

Event

Abstract

Tae1 is an amidase produced by gram negative Pseudomonas bacteria that attacks the peptidoglycan layer in the cell walls of neighboring bacteria after secretion through the Type VI secretion system (T6S). The goal of our work is mapping interactions between the type-VI-secretion system effector Tae1 and its putative substrates using nuclear magnetic resonance (NMR) spectroscopy. Tae1 is amenable to NMR in that we are able to gather spectra with resolved, well defined peaks that can be assigned providing valuable structural information. We have been able to achieve nearly complete assignment of the backbone atoms, and roughly 85% coverage for the side-chain atoms of Tae1 via 15N-HSQC, HCCH COSY, HCCH TOCSY, and HCONH TOCSY experiments. Current work is focused on interpreting data from binding experiments of Tae1 with peptidoglycan via 13C-HSQC. From these binding experiments we hope to better understand the peptidoglycan cleavage specificity of Tae1.

Rights

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Language

English

Format

application/pdf

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May 14th, 10:00 AM May 14th, 2:00 PM

Mapping interactions between the type-VI secretion system effector Tae1 and its putative substrates using NMR spectroscopy

Chemistry

Tae1 is an amidase produced by gram negative Pseudomonas bacteria that attacks the peptidoglycan layer in the cell walls of neighboring bacteria after secretion through the Type VI secretion system (T6S). The goal of our work is mapping interactions between the type-VI-secretion system effector Tae1 and its putative substrates using nuclear magnetic resonance (NMR) spectroscopy. Tae1 is amenable to NMR in that we are able to gather spectra with resolved, well defined peaks that can be assigned providing valuable structural information. We have been able to achieve nearly complete assignment of the backbone atoms, and roughly 85% coverage for the side-chain atoms of Tae1 via 15N-HSQC, HCCH COSY, HCCH TOCSY, and HCONH TOCSY experiments. Current work is focused on interpreting data from binding experiments of Tae1 with peptidoglycan via 13C-HSQC. From these binding experiments we hope to better understand the peptidoglycan cleavage specificity of Tae1.