Evidence map›Paper›PMID 30266969›Full record

ArticleNature communications2018

Towards a comprehensive understanding of the structural dynamics of a bacterial diterpene synthase during catalysis.

Ronja Driller, Sophie Janke, Monika Fuchs, Evelyn Warner, Anil R Mhashal, Dan Thomas Major, Mathias Christmann, Thomas Brück, Bernhard Loll

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
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  4. The initial dynamics of product release in terpene synthases-The case of CotB2.Protein science : a publication of the Protein Society · 2025
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  5. Article
  6. CHARMM-GUIJournal of chemical theory and computation · 2025
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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.

Ronja DrillerInstitut für Chemie und Biochemie, Strukturbiochemie, Freie Universität Berlin, Takustr. 6, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0001-8834-9087
Sophie JankeInstitut für Chemie und Biochemie, Organische Chemie, Freie Universität Berlin, Takustr. 3, 14195, Berlin, Germany.
Monika FuchsWerner Siemens Chair of Synthetic Biotechnology, Department of Chemistry, Technical University of Munich (TUM), Lichtenbergstr. 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0002-6954-2639
Evelyn WarnerInstitut für Chemie und Biochemie, Organische Chemie, Freie Universität Berlin, Takustr. 3, 14195, Berlin, Germany.
Anil R MhashalDepartment of Chemistry, Bar-Ilan University, Ramat-Gan, 52900, Israel.ORCID http://orcid.org/0000-0002-8232-8135
Dan Thomas MajorDepartment of Chemistry, Bar-Ilan University, Ramat-Gan, 52900, Israel.ORCID http://orcid.org/0000-0002-9231-0676
Mathias ChristmannInstitut für Chemie und Biochemie, Organische Chemie, Freie Universität Berlin, Takustr. 3, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0001-9313-2392
Thomas BrückWerner Siemens Chair of Synthetic Biotechnology, Department of Chemistry, Technical University of Munich (TUM), Lichtenbergstr. 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0002-2113-6957
Bernhard LollInstitut für Chemie und Biochemie, Strukturbiochemie, Freie Universität Berlin, Takustr. 6, 14195, Berlin, Germany. loll@chemie.fu-berlin.de.ORCID http://orcid.org/0000-0001-7928-4488

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terpenes constitute the largest and structurally most diverse natural product family. Most terpenoids exhibit a stereochemically complex macrocyclic core, which is generated by C-C bond forming of aliphatic oligo-prenyl precursors. This reaction is catalysed by terpene synthases (TPSs), which are capable of chaperoning highly reactive carbocation intermediates through an enzyme-specific reaction. Due to the instability of carbocation intermediates, the proteins' structural dynamics and enzyme:substrate interactions during TPS catalysis remain elusive. Here, we present the structure of the diterpene synthase CotB2, in complex with an in crystallo cyclised abrupt reaction product and a substrate-derived diphosphate. We captured additional snapshots of the reaction to gain an overview of CotB2's catalytic mechanism. To enhance insights into catalysis, structural information is augmented with multiscale molecular dynamic simulations. Our data represent fundamental TPS structure dynamics during catalysis, which ultimately enable rational engineering towards tailored terpene macrocycles that are inaccessible by conventional chemical synthesis.

Indexed as

Molecular Dynamics SimulationAlkyl and Aryl TransferasesBacterial ProteinsBiocatalysisCrystallography, X-RayCyclizationDiterpenesModels, ChemicalMolecular StructureMutationAlkyl and Aryl TransferasesBacterial ProteinsDiterpenesterpene synthase

Identifiers

PMID30266969
PMCPMC6162201

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Registered trials

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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.