Evidence map›Paper›PMID 41634007›Full record

ArticleNature communications2026

Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.

Hu Xiao, Shanqin Li, Ruxi Qi, Yuxiang Hu, Xiaozi Jiang, Jing Luo, Jing Wu, Lei Zhang, Shuman Xu, Defen Lu and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Hu Xiao *School of Life Sciences, Southwest United Graduate School, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China.
Shanqin Li *Institute of Pediatrics, Shenzhen Children's Hospital, Shenzhen, Guangdong, China.
Ruxi Qi *Cryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Yuxiang HuSchool of Life Sciences, Southwest United Graduate School, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China.
Xiaozi JiangSchool of Life Sciences, Southwest United Graduate School, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China.
Jing LuoSchool of Life Sciences, Southwest United Graduate School, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China.
Jing WuCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Lei ZhangCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0002-0515-5576
Shuman XuCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Defen LuCollege of Life Sciences, Shanxi Agricultural University, Taiyuan, China. ludefen1@sxau.edu.cn.
Xinwang YangDepartment of Anatomy and Histology & Embryology, Faculty of Basic Medical Science, Kunming Medical University, Kunming, Yunnan, China. yangxinwanghp@163.com.ORCID 0000-0003-3210-8908
Qingfeng ChenSchool of Life Sciences, Southwest United Graduate School, Yunnan Key Laboratory of Cell Metabolism and Diseases, State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China. qingfengchen@ynu.edu.cn.ORCID 0000-0001-9526-0806
Sheng LiuInstitute of Pediatrics, Shenzhen Children's Hospital, Shenzhen, Guangdong, China. sliu520@mail.ustc.edu.cn.

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32071202
6 · The paper itself

Abstract

Inorganic phosphate (Pi) is essential for all living organisms. PstSCAB, a bacterial high-affinity ABC transporter, imports Pi under limiting conditions via five subunits: PstA and PstC forming the transmembrane domain (TMD), periplasmic PstS that switches between free and TMD-docked forms for Pi capture and delivery, and two cytosolic PstB subunits for ATP binding and hydrolysis. Its malfunction affects the virulence of pathogenic bacteria, making it pharmaceutically attractive. However, complete structural pictures of PstSCAB in different states remain lacking. Here, we determine cryo-EM structures of PstSCAB in resting, pretranslocation, and catalytic intermediate states, which reveal that conformational changes in PstS and ATP binding/unbinding in PstB collectively induce rigid-body movements of TMD, generating inward- or outward-facing conformations. In TMD, Pi specificity is determined by positively charged Arg220 (PstA) and Arg237 (PstC). This study advances understanding of bacterial Pi import and supports drug development targeting PstSCAB.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsPhosphatesAdenosine TriphosphateBiological TransportCryoelectron MicroscopyModels, MolecularProtein BindingProtein ConformationProtein DomainsAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsPhosphates

Identifiers

PMID41634007
PMCPMC12976172

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.