Evidence map›Paper›PMID 33257858›Full record

ArticleNature plants2020

The active site of magnesium chelatase.

Nathan B P Adams, Claudine Bisson, Amanda A Brindley, David A Farmer, Paul A Davison, James D Reid, C Neil Hunter

Abstract read
PubMed Publisher
In one paragraph

Article in Nature plants, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. QTL mapping and candidate gene analysis reveal two major loci regulating green leaf color in non-heading Chinese cabbage.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  8. Article
  9. Frontiers in plant science · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors.

Nathan B P Adams *Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK. nathan.adams@sheffield.ac.uk.ORCID http://orcid.org/0000-0003-3080-3448
Claudine Bisson *Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK.ORCID http://orcid.org/0000-0002-9430-6822
Amanda A BrindleyDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK.
David A FarmerDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK.ORCID http://orcid.org/0000-0001-5331-3551
Paul A DavisonDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK.ORCID http://orcid.org/0000-0002-5931-8326
James D ReidDepartment of Chemistry, The University of Sheffield, Sheffield, UK.ORCID http://orcid.org/0000-0003-4921-1047
C Neil HunterDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, UK. c.n.hunter@sheffield.ac.uk.ORCID http://orcid.org/0000-0003-2533-9783

Funding

Biotechnology and Biological Sciences Research Council BB/M000265/1Biotechnology and Biological Sciences Research Council BB/M011151/1
6 · The paper itself

Abstract

The insertion of magnesium into protoporphyrin initiates the biosynthesis of chlorophyll, the pigment that underpins photosynthesis. This reaction, catalysed by the magnesium chelatase complex, couples ATP hydrolysis by a ChlID motor complex to chelation within the ChlH subunit. We probed the structure and catalytic function of ChlH using a combination of X-ray crystallography, computational modelling, mutagenesis and enzymology. Two linked domains of ChlH in an initially open conformation of ChlH bind protoporphyrin IX, and the rearrangement of several loops envelops this substrate, forming an active site cavity. This induced fit brings an essential glutamate (E660), proposed to be the key catalytic residue for magnesium insertion, into proximity with the porphyrin. A buried solvent channel adjacent to E660 connects the exterior bulk solvent to the active site, forming a possible conduit for the delivery of magnesium or abstraction of protons.

Indexed as

Enzyme ActivationChlorophyllLyasesPhotosynthesisProtoporphyrinsThermosynechococcusChlorophyllLyasesmagnesium chelataseProtoporphyrins

Identifiers

PMID33257858

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.