# Structures of Cutibacterium acnes hyaluronate lyases suggest a correlation between active site opened/closed state and conformation of abutting loop

## TL;DR

This paper explores how the shape of a loop in a bacterial enzyme correlates with the opening or closing of its active site.

## Contribution

The study reveals a structural correlation between a loop's conformation and the active site state in hyaluronate lyases.

## Key findings

- Open structures of hyaluronate lyases correlate with a specific loop conformation.
- Closed structures correlate with a different loop conformation.
- Mutations in the loop did not significantly impact enzyme activity.

## Abstract

The structures of hyaluronate lyases from two
Cutibacterium acnes
strains
have been reported recently and show open catalytic clefts. We compared these open structures with more closed structures of homologous lyases and found that the conformation of a loop that abuts the catalytic cleft is seemingly correlated with the opening and closing of the cleft. We illustrate that the loop conformation seen in the open lyase appears incompatible with a closed catalytic cleft, and vice versa; however, mutations designed to disrupt the loop conformation did not significantly affect catalytic activity.