ArticleNature2018
Structure of the peptidoglycan polymerase RodA resolved by evolutionary coupling analysis.
Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
What it found
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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.
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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.
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Who cites it
75 citing papers in PubMed, 138 citations in OpenAlex.
- RodZ acts through MreBCD to activate the elongasome inJournal of bacteriology · 2026Article
- Direct interaction between MreB and the RodA-PBP2 complex organizes lateral cell wall synthesis inmLife · 2026Article
- AlphaFold as a prior: experimental structure determination conditioned on a pretrained neural network.Nature methods · 2026Article
- Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026Review
- SEDS glycosyltransferases inmSphere · 2025Article
- Selection of nanobodies against liponanoparticle-embedded membrane proteins by yeast-surface display.Protein science : a publication of the Protein Society · 2025Article
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- The hit-and-run of cell wall synthesis: LpoB transiently binds and activates PBP1b through a conserved allosteric switch.Nature communications · 2025Article
- Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025Review
- Article
- Peptidoglycan Endopeptidase PBP7 Facilitates the Recruitment of FtsN to the Divisome and Promotes Peptidoglycan Synthesis in Escherichia coli.Molecular microbiology · 2024Article
- Pbp4 provides transpeptidase activity to the FtsW-PbpB peptidoglycan synthase to drive cephalosporin resistance inAntimicrobial agents and chemotherapy · 2024Article
- Elongasome core proteins and class A PBP1a display zonal, processive movement at the midcell ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Diversity of sugar-diphospholipid-utilizing glycosyltransferase families.Communications biology · 2024Article
- Article
- Structural insights into the activation of the divisome complex FtsWIQLB.Cell discovery · 2024Article
- Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.Nature communications · 2023Article
- The relaxin receptor RXFP1 signals through a mechanism of autoinhibition.Nature chemical biology · 2023Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
The shape, elongation, division and sporulation (SEDS) proteins are a large family of ubiquitous and essential transmembrane enzymes with critical roles in bacterial cell wall biology. The exact function of SEDS proteins was for a long time poorly understood, but recent work has revealed that the prototypical SEDS family member RodA is a peptidoglycan polymerase-a role previously attributed exclusively to members of the penicillin-binding protein family. This discovery has made RodA and other SEDS proteins promising targets for the development of next-generation antibiotics. However, little is known regarding the molecular basis of SEDS activity, and no structural data are available for RodA or any homologue thereof. Here we report the crystal structure of Thermus thermophilus RodA at a resolution of 2.9 Å, determined using evolutionary covariance-based fold prediction to enable molecular replacement. The structure reveals a ten-pass transmembrane fold with large extracellular loops, one of which is partially disordered. The protein contains a highly conserved cavity in the transmembrane domain, reminiscent of ligand-binding sites in transmembrane receptors. Mutagenesis experiments in Bacillus subtilis and Escherichia coli show that perturbation of this cavity abolishes RodA function both in vitro and in vivo, indicating that this cavity is catalytically essential. These results provide a framework for understanding bacterial cell wall synthesis and SEDS protein function.
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Registered trials
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 OpenQuestion graph.