Evidence map›Paper›PMID 36322423›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Crystal structure of the capsular polysaccharide-synthesis enzyme CapG from Staphylococcus aureus.

Ni Tien, Chien Yi Ho, Shu Jung Lai, Yu Chuan Lin, Chia Shin Yang, Yu Chuan Wang, Wei Chien Huang, Yeh Chen, Jui Jen Chang

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 53% of its field
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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

9 authors at 2 institutions in 1 country.

Ni TienDepartment of Laboratory Medicine, China Medical University Hospital, Taichung, Taiwan.ORCID 0000-0003-3754-184X
Chien Yi HoDepartment of Biomedical Imaging and Radiological Science, China Medical University, Taichung, Taiwan.
Shu Jung LaiGraduate Institute of Biomedical Sciences, China Medical University, Taichung, Taiwan.
Yu Chuan LinTranslational Cell Therapy Center, China Medical University Hospital, Taichung, Taiwan.ORCID 0000-0002-9580-7418
Chia Shin YangInstitute of Translational Medicine and New Drug Development, China Medical University, Taichung, Taiwan.
Yu Chuan WangInstitute of Translational Medicine and New Drug Development, China Medical University, Taichung, Taiwan.ORCID 0000-0003-2726-9731
Wei Chien HuangGraduate Institute of Biomedical Sciences, China Medical University, Taichung, Taiwan.ORCID 0000-0001-6467-8716
Yeh ChenInstitute of Translational Medicine and New Drug Development, China Medical University, Taichung, Taiwan.ORCID 0000-0002-7740-0446
Jui Jen ChangGraduate Institute of Integrated Medicine, China Medical University, Taichung, Taiwan.
China Medical University · TWAsia University · TW

Funding

Ministry of Science and Technology, Taiwan 111-2311-B-039-001-MY3Ministry of Science and Technology, Taiwan CMU111-MF-06
6 · The paper itself

Abstract

Bacterial capsular polysaccharides provide protection against environmental stress and immune evasion from the host immune system, and are therefore considered to be attractive therapeutic targets for the development of anti-infectious reagents. Here, we focused on CapG, one of the key enzymes in the synthesis pathway of capsular polysaccharides type 5 (CP5) from the opportunistic pathogen Staphylococcus aureus. SaCapG catalyses the 2-epimerization of UDP-N-acetyl-D-talosamine (UDP-TalNAc) to UDP-N-acetyl-D-fucosamine (UDP-FucNAc), which is one of the nucleotide-activated precursors for the synthesis of the trisaccharide repeating units of CP5. Here, the cloning, expression and purification of recombinant SaCapG are reported. After extensive efforts, single crystals of SaCapG were successfully obtained which belonged to space group C2 and exhibited unit-cell parameters a = 302.91, b = 84.34, c = 145.09 Å, β = 110.65°. The structure was solved by molecular replacement and was refined to 3.2 Å resolution. The asymmetric unit revealed a homohexameric assembly of SaCapG, which was consistent with gel-filtration analysis. Structural comparison with UDP-N-acetyl-D-glucosamine 2-epimerase from Methanocaldococcus jannaschii identified α2, the α2-α3 loop and α10 as a gate-regulated switch controlling substrate entry and/or product release.

Indexed as

Polysaccharides, BacterialStaphylococcus aureusCrystallography, X-RayMethanocaldococcusUridine DiphosphatePolysaccharides, BacterialUridine Diphosphate2-epimerasesCapGcapsular polysaccharidescrystal structureStaphylococcus aureus

Identifiers

PMID36322423
PMCPMC9629516
OpenAlexW4306252936

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.