{
  "id": 5270547,
  "title": "X-ray crystallographic fragment screening reveals novel and conformationally dynamic ligand-binding sites in Mycobacterium tuberculosis FtsZ",
  "url": "https://urgent.news/2026/09/02/x-ray-crystallographic-fragment-screening-reveals-novel-and",
  "topic": "health",
  "section": "Health & Medicine",
  "published": "2026-09-02T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748605v1?rss=1"
  },
  "original_language": "en",
  "account": "Tuberculosis claims countless lives annually due to the infectious agent it harbors. There remains a pressing need for innovative ways to curb M. tuberculosis (Mtb) proliferation and infection to enhance patient prognosis. FtsZ, a GTPase that assembles into protofilaments at the division site of a proliferating cell, resulting in two distinct cells, emerges as a promising target due to its essential role in bacterial cell division. This study details a crystallographic fragment screening initiative of MtbFtsZ, involving the soaking of 1,070 crystals with fragment samples and the utilization of 714 datasets for subsequent PanDDA analysis. Out of these, 149 datasets demonstrated PanDDA-generated event map density, facilitating the modeling of fragment binding. Fifteen novel binding sites are unveiled, with both the ON and OFF conformations of FtsZ present in the asymmetric unit. The crystallographic fragment screening also offers prospects for expanding and merging fragments to transform FtsZ binders into drug-like molecules or specific chemical probes that mimic conformation.",
  "summary": "Tuberculosis is a leading cause of death globally due to an infectious agent. There is ongoing need for novel mechanisms to inhibit M. tuberculosis (Mtb) growth and infection to improve patient outcomes. FtsZ, a GTPase that assembles into protofilaments at the division site of a replicating cell to produce two individual cells, is an attractive target as an essential protein in bacterial cell…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 2,
    "also_reported_by": [
      {
        "outlet": "bioRxiv",
        "title": "A conserved cysteine-histidine-glutamate metal site identifies DUF501 (Rv1025), an essential uncharacterised protein family of Mycobacterium tuberculosis, as a candidate metalloenzyme and drug target",
        "url": "https://urgent.news/2026/09/03/a-conserved-cysteine-histidine-glutamate-metal-site-identifies-duf501",
        "published": "2026-09-03T00:00:00.000Z"
      }
    ]
  },
  "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."
}