Evidence map›Paper›PMID 32632294›Full record

ArticleNature chemical biology2020

Architecture and functional dynamics of the pentafunctional AROM complex.

Harshul Arora Verasztó, Maria Logotheti, Reinhard Albrecht, Alexander Leitner, Hongbo Zhu, Marcus D Hartmann

Abstract read
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In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Hybrid Chemoenzymatic Synthesis of CChembiochem : a European journal of chemical biology · 2022
    Article
  7. Review
  8. Channeling a complex question.Nature chemical biology · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Harshul Arora VerasztóDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID http://orcid.org/0000-0002-0702-6022
Maria LogothetiDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Reinhard AlbrechtDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Alexander LeitnerDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4126-0725
Hongbo ZhuDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Marcus D HartmannDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany. marcus.hartmann@tuebingen.mpg.de.ORCID http://orcid.org/0000-0001-6937-5677
Max Planck Institute for Developmental Biology · DEETH Zurich · CHUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The AROM complex is a multifunctional metabolic machine with ten enzymatic domains catalyzing the five central steps of the shikimate pathway in fungi and protists. We determined its crystal structure and catalytic behavior, and elucidated its conformational space using a combination of experimental and computational approaches. We derived this space in an elementary approach, exploiting an abundance of conformational information from its monofunctional homologs in the Protein Data Bank. It demonstrates how AROM is optimized for spatial compactness while allowing for unrestricted conformational transitions and a decoupled functioning of its individual enzymatic entities. With this architecture, AROM poses a tractable test case for the effects of active site proximity on the efficiency of both natural metabolic systems and biotechnological pathway optimization approaches. We show that a mere colocalization of enzymes is not sufficient to yield a detectable improvement of metabolic throughput.

Indexed as

3-Phosphoshikimate 1-CarboxyvinyltransferaseAcanthamoeba castellaniiCatalytic DomainChaetomiumFungal ProteinsModels, MolecularMultienzyme ComplexesPhosphorus-Oxygen LyasesProtein ConformationProtein DomainsScattering, Small AngleShikimic AcidToxoplasmaX-Ray Diffraction3-dehydroquinate synthetase3-Phosphoshikimate 1-CarboxyvinyltransferaseFungal ProteinsMultienzyme ComplexesPhosphorus-Oxygen LyasesShikimic Acid

Identifiers

PMID32632294
OpenAlexW3038460069

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.