# X-Ray Crystal Structure of the N-Terminal Domain of Staphylococcus Aureus Cell-Cycle Protein GpsB

## TL;DR

This paper reports the crystal structure of a key cell-cycle protein in Staphylococcus aureus, revealing its unique shape and role in cell division.

## Contribution

The study provides a high-resolution structure of the N-terminal domain of S. aureus GpsB, confirming its unique conformation and role in cell division.

## Key findings

- The N-terminal domain of S. aureus GpsB forms an asymmetric dimer with a bent conformation.
- The structure matches one of two conformations previously reported, validating the unique fold of S. aureus GpsB.
- The findings support GpsB's role in organizing the cell division machinery in S. aureus.

## Abstract

GpsB is a conserved cell-cycle regulator in the Firmicute clade of Gram-positive bacteria that coordinates multiple aspects of envelope biogenesis. Recent studies demonstrate interactions between GpsB and the key division cytoskeleton FtsZ, suggesting that GpsB links cell division to various aspects of cell envelope biogenesis in Staphylococcus aureus and potentially other Firmicutes. We determined a 1.7 Å resolution crystal structure of the N-terminal domain of Staphylococcus aureus GpsB, revealing an asymmetric dimer with a bent conformation. This conformation is nearly identical to one of two conformations reported by Sacco, et al., confirming the unique conformation of S. aureus GpsB compared to other gram-positive bacteria. This structural agreement provides strong validation of the S. aureus GpsB fold and supports its proposed role in organizing the cell division machinery.