# The Crystal Structure of the Domain of Unknown Function 1480 (DUF1480) From Klebsiella pneumoniae

## TL;DR

This paper reports the first crystal structure of the DUF1480 protein from Klebsiella pneumoniae, offering insights into its potential role in antibiotic response.

## Contribution

The paper provides the first experimental crystal structure of the DUF1480 domain, revealing its structural features and potential functional relevance.

## Key findings

- DUF1480 has a six-stranded split barrel fold with a small alpha helix capping one end.
- DUF1480 is monomeric in solution and structurally similar to response regulators.
- The structure reveals conserved features that may be important for its function.

## Abstract

Domains of unknown function (DUFs) continue to comprise a significant portion of bacterial proteomes, with more than 20% of bacterial proteins remaining annotated as DUFs. The characterization of their molecular structure can provide valuable insight that is not captured by the primary sequence analysis, thus providing a segue into the identification of the molecular function of DUF representatives. Here, we present the crystal structure of KPN_02352 from Klebsiella pneumoniae subsp. pneumoniae, a DUF1480 domain‐containing protein, which was determined to be 1.75 Å resolution. Representatives of the DUF1480 family are found broadly across Enterobacterales and have been previously shown to contribute to the antibiotic response. Our structural analysis suggests that DUF1480 is comprised of a six‐stranded split barrel fold featuring a small alpha helix that is positioned to cap one end of the split barrel. DUF1480 was found to be monomeric in solution, and harbors structural similarity to response regulators. The crystal structure of DUF1480 is the first experimental insight into the molecular structure of this conserved protein family, revealing several conserved features that may be functionally relevant.