{
  "id": 102609,
  "title": "β-Propeller structure of the CJ1041C protein from Campylobacter jejuni and its interaction with Ca 2+ ions",
  "url": "https://urgent.news/2026/08/03/propeller-structure-of-the-cj1041c-protein-from-campylobacter-jejuni",
  "topic": "science",
  "section": "Science",
  "published": "2026-08-03T00:00:00.000Z",
  "source": {
    "name": "Scientific Reports",
    "slug": "scientific-reports",
    "url": "https://www.nature.com/articles/s41598-026-64794-0"
  },
  "original_language": "en",
  "account": "Campylobacter jejuni, the primary bacterial cause of foodborne enteric disease globally, poses a significant health threat due to the rising presence of antibiotic-resistant strains. Identifying novel protein targets for antibacterial drug development becomes crucial through the functional analysis of lesser-studied C. jejuni proteins. One such protein is CJ1041C, whose role remains unexplored experimentally. To investigate CJ1041C, researchers determined its crystal structures in both apo form and complex with Ca2+ ions. The protein exhibits a six-bladed β-propeller architecture, characterized by six four-stranded β-sheets arranged around a central channel. In the apo form, this channel is closed and contains two negatively charged cavities. The upper cavity specifically coordinates a Ca2+ ion through conserved residues and also accommodates a glycerol molecule, which may act as a substrate–water mimic. The Ca2+-binding configuration of CJ1041C mirrors that observed in β-propeller lactonases, implying that the protein functions as a lactonase or lactonase-like enzyme. However, the unique glycerol-binding mode of CJ1041C, along with phylogenetic and sequence analyses, suggests that it is a distinct member of the β-propeller lactonase family. This protein likely possesses catalytic activity towards noncanonical substrates. The authors acknowledge the support from the National Research Foundation of Korea and the ANCHOR program.",
  "summary": "Scientific Reports, Published online: 03 August 2026; doi:10.1038/s41598-026-64794-0 β-Propeller structure of the CJ1041C protein from Campylobacter jejuni and its interaction with Ca 2+ ions",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 2,
    "also_reported_by": [
      {
        "outlet": "bioRxiv",
        "title": "Efficient colonic colonization by Campylobacter jejuni requires the heme receptor ChuA",
        "url": "https://urgent.news/2026/08/04/efficient-colonic-colonization-by-campylobacter-jejuni-requires-the",
        "published": "2026-08-04T00:00:00.000Z"
      }
    ]
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}