RESEARCH: CANCER
FOLDING PROJECT #18927 PROFILE

This project looks at how a special enzyme called ProcM picks the right spot to attach parts of a tiny protein. Scientists want to use this knowledge to design new medicines using these proteins, but they don't know exactly how ProcM works. So they are doing computer simulations to see how ProcM interacts with different parts of the protein.

Lanthipeptides are ribosomally synthesized and post-translationally modified peptides that are generated from precursor peptides through a dehydration and cyclization process.

Lanthipeptides have demonstrated a variety of bioactivities, including anticancer, antimicrobial, antiviral, and antiallodynic activities.

ProcM, a class II lanthipeptide synthetase, demonstrates high substrate tolerance.

It is enigmatic that a single enzyme can catalyze the cyclization process of many substrates with high fidelity.

This feature has been widely utilized for bioengineering of novel lanthipeptides.

However, the molecular mechanism about how ProcM determines site-selectivity of its substrates is still unclear.

In this study, we would like to run atomic-level MD simulation for WT and Variant ProcM-ProcA3.3 complex to explore the site-selectivity of ProcM.

Lanthipeptides

Ribosomally synthesized and post-translationally modified peptides.

Lanthipeptides are a class of antibiotics produced by bacteria. They are characterized by their unique structure, which includes the presence of dehydrated amino acids (lanthionine rings). Lanthipeptides have shown promising activity against a range of bacterial infections and are being investigated for potential use in new antimicrobial therapies.

ProcM

ProcM: Class II lanthipeptide synthetase.

ProcM is an enzyme that plays a crucial role in the biosynthesis of lanthipeptides. Specifically, it catalyzes the cyclization process, which is essential for forming the characteristic structure of these antibiotics. Researchers are interested in understanding the mechanism of ProcM and how it recognizes its substrates to potentially engineer new lanthipeptides with improved properties.

MD Simulation

Molecular Dynamics Simulation

MD simulation is a computer-based method used to simulate the movement of atoms and molecules over time. This technique helps researchers understand how biomolecules interact and behave in complex environments. In the context of ProcM research, MD simulations are likely being used to explore how the enzyme interacts with its substrates at an atomic level.

Variant

A mutated or altered form of a protein.

Variants are different versions of a protein that may have subtle changes in their amino acid sequence. These variations can alter the protein's function, stability, or interactions with other molecules. In this study, researchers are likely investigating how mutations in ProcM affect its site-selectivity.

Site-Selectivity

The ability of an enzyme to bind to and modify specific substrates.

Site-selectivity refers to the enzyme's ability to choose particular substrates from a mixture. In the case of ProcM, understanding its site-selectivity is crucial for designing new lanthipeptides with desired properties.