Evidence map›Paper›PMID 26750487›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Structure of methionine γ-lyase from Clostridium sporogenes.

Svetlana Revtovich, Natalya Anufrieva, Elena Morozova, Vitalia Kulikova, Alexey Nikulin, Tatyana Demidkina

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

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural Basis of the Inhibition of L-Methionine γ-Lyase fromInternational journal of molecular sciences · 2023
    Article
  4. Canavanine utilizationRSC chemical biology · 2022
    Article
  5. Article
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

6 authors at 1 institution in 1 country.

Svetlana RevtovichEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Natalya AnufrievaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Elena MorozovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Vitalia KulikovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Alexey NikulinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Tatyana DemidkinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
Engelhardt Institute of Molecular Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methionine γ-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the γ-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 Å resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii, Entamoeba histolytica, Pseudomonas putida and Trichomonas vaginalis. A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture.

Indexed as

Bacterial ProteinsCarbon-Sulfur LyasesCatalytic DomainClostridiumCrystallizationCrystallography, X-RayHydrogen BondingKineticsMethionineModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein Structure, QuaternaryPyridoxal PhosphateBacterial ProteinsCarbon-Sulfur LyasesL-methionine gamma-lyaseMethioninePyridoxal Phosphateactive siteClostridium sporogenesmethionine γ-lyasepyridoxal 5′-phosphate-binding sitetetrameric contacts

Identifiers

PMID26750487
PMCPMC4708053
OpenAlexW2337311192

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.