ArticleProtein science : a publication of the Protein Society2025
Protein-tags and their fragments as potent inhibitors of enzymes: Structure of the ternary complex of phosphopantetheine adenylyltransferase from Enterobacter spp. with tag-peptides and phosphonoacetic acid at 2.20 Å resolution.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Article
- Protein-tags and their fragments as potent inhibitors of enzymes: Structure of the ternary complex of phosphopantetheine adenylyltransferase from Enterobacter spp. with tag-peptides and phosphonoacetic acid at 2.20 Å resolution.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step of coenzyme A (CoA) biosynthesis pathway by transferring the adenylyl group from adenosine triphosphate (ATP) to 4'-phosphopantetheine (PNS), yielding 3'-dephosphocoenzyme A and pyrophosphate. In this study, the recombinant PPAT from Enterobacter spp. strain 638 (EbPPAT) was purified and co-crystallized with phosphonoacetic acid (PAE). The structure showed the presence of three homodimers AB, CD, and EF in the asymmetric unit. The 14 extra N-terminal residues (Met-14 to Ser-1, 14-mer peptide) from the expression tag were observed in Molecules B and F. These tag-peptides occupied the PNS-binding sites of adjacent Molecules A and E, respectively. Additionally, a heptapeptide (Met-14 to Gly-8) was also observed in the PNS-binding site of Molecule C. Furthermore, two PAE molecules were present in the ATP-binding sites of Molecules B, D, and F, whereas a single PAE molecule was found in Molecules A, C, and E. This showed that tag-peptides blocked the PNS-binding site while PAE blocked the ATP-binding sites. Three peptides of the tag, including 14-mer (Met-14 to Ser-1), heptapeptide (Met-14 to Gly-8) and pentapeptide (Met-14 to Thr-10) were synthesized, and their binding affinities were estimated, which showed the K
Indexed as
Identifiers
What OpenQuestion holds
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.