Evidence map›Paper›PMID 33682790›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Crystal structures of anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae.

Xiaofei Wu, Mengying Zhang, Zhiling Kuang, Jian Yue, Lu Xue, Min Zhu, Zhongliang Zhu, Muhammad Hidayatullah Khan, Liwen Niu

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

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    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

9 authors at 1 institution in 1 country.

Xiaofei WuSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Mengying ZhangSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Zhiling KuangSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Jian YueSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Lu XueSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Min ZhuSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Zhongliang ZhuSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Muhammad Hidayatullah KhanSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.ORCID 0000-0003-1703-164X
Liwen NiuSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
University of Science and Technology of China · CN

Funding

Ministry of Science and Technology of the People's Republic of China 2017YFA0504903National Natural Science Foundation of China 31621002
6 · The paper itself

Abstract

Anthranilate phosphoribosyltransferase (AnPRT) catalyzes the transfer of the phosphoribosyl group of 5'-phosphoribosyl-1'-pyrophosphate (PRPP) to anthranilate to form phosphoribosyl-anthranilate. Crystal structures of AnPRTs from bacteria and archaea have previously been determined; however, the structure of Saccharomyces cerevisiae AnPRT (ScAnPRT) still remains unsolved. Here, crystal structures of ScAnPRT in the apo form as well as in complex with its substrate PRPP and the substrate analogue 4-fluoroanthranilate (4FA) are presented. These structures demonstrate that ScAnPRT exhibits the conserved structural fold of type III phosphoribosyltransferase enzymes and shares the similar mode of substrate binding found across the AnPRT protein family. In addition, crystal structures of ScAnPRT mutants (ScAnPRT

Indexed as

Amino Acid MotifsAmino Acid SequenceAnthranilate PhosphoribosyltransferaseBinding SitesConserved SequenceCrystallography, X-RayDiphosphatesortho-AminobenzoatesProtein MultimerizationProtein Structure, SecondarySaccharomyces cerevisiaeAnthranilate Phosphoribosyltransferaseanthranilic acidDiphosphatesdiphosphoric acidortho-Aminobenzoatesanthranilate phosphoribosyltransferasecrystal structureSaccharomyces cerevisiaesubstrate binding

Identifiers

PMID33682790
PMCPMC7938636
OpenAlexW3134161647

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.