8IEV

Crystal structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni in space group C2

8IEV の概要

• エントリーDOI: 10.2210/pdb8iev/pdb
• 関連するPDBエントリー: 8IEU
• 分子名称: DUF2891 domain-containing protein (2 entities in total)
• 機能のキーワード: duf2891, unknown function
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 236593.48

構造登録者

Kim, S.Y.,Cho, H.Y.,Yoon, S.I. (登録日: 2023-02-16, 公開日: 2023-05-31, 最終更新日: 2024-05-29)

主引用文献

Kim, S.Y.,Cho, H.Y.,Yoon, S.I.
Unique dimeric structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni.
Biochem.Biophys.Res.Commun., 655:11-17, 2023

PubMed Abstract: Campylobacter jejuni is a pathogenic bacterium that causes enteritis and Guillain-Barre syndrome in humans. To identify a protein target for the development of a new therapeutic against C. jejuni infection, each gene product of C. jejuni must be functionally characterized. The cj0554 gene of C. jejuni encodes a DUF2891 family protein with unknown functions. To provide functional insights into CJ0554, we determined and analyzed the crystal structure of the CJ0554 protein. CJ0554 adopts an (α/α)-barrel structure, which consists of an inner α ring and an outer α ring. CJ0554 assembles into a dimer in a unique top-to-top orientation that is not observed in its structural homologs, N-acetylglucosamine 2-epimerase superfamily members. Dimer formation was verified by analyzing CJ0554 and its ortholog protein through gel-filtration chromatography. The top of the CJ0554 monomer barrel harbors a cavity, which is connected to that of the second subunit in the dimer structure, generating a larger intersubunit cavity. This elongated cavity accommodates extra nonproteinaceous electron density, presumably as a pseudosubstrate, and is lined with generally catalytically active histidine residues that are invariant in CJ0554 orthologs. Therefore, we propose that the cavity functions as the active site of CJ0554.

PubMed: 36913761
DOI: 10.1016/j.bbrc.2023.03.010

実験手法

X-RAY DIFFRACTION (2.08 Å)