Evidence map›Paper›PMID 28291751›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

The hyperthermophilic cystathionine γ-synthase from the aerobic crenarchaeon Sulfolobus tokodaii: expression, purification, crystallization and structural insights.

Dan Sato, Tomoo Shiba, Sae Mizuno, Ayaka Kawamura, Shoko Hanada, Tetsuya Yamada, Mai Shinozaki, Masahiko Yanagitani, Takashi Tamura, Kenji Inagaki and 1 more

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

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

11 authors at 3 institutions in 1 country.

Dan SatoDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Tomoo ShibaDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Sae MizunoDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Ayaka KawamuraDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Shoko HanadaDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Tetsuya YamadaDepartment of Biofunctional Chemistry, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama 700-8530, Japan.
Mai ShinozakiDepartment of Biofunctional Chemistry, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama 700-8530, Japan.
Masahiko YanagitaniDepartment of Biofunctional Chemistry, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama 700-8530, Japan.
Takashi TamuraDepartment of Biofunctional Chemistry, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama 700-8530, Japan.
Kenji InagakiDepartment of Biofunctional Chemistry, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama 700-8530, Japan.
Shigeharu HaradaDepartment of Applied Biology, Kyoto Institute of Technology, Gosho Kaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
Okayama University · JPOsaka University · JPKyoto Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystathionine γ-synthase (CGS; EC 2.5.1.48), a pyridoxal 5'-phosphate (PLP)-dependent enzyme, catalyzes the formation of cystathionine from an L-homoserine derivative and L-cysteine in the first step of the transsulfuration pathway. Recombinant CGS from the thermoacidophilic archaeon Sulfolobus tokodaii (StCGS) was overexpressed in Escherichia coli and purified to homogeneity by heat treatment followed by hydroxyapatite and gel-filtration column chromatography. The purified enzyme shows higher enzymatic activity at 353 K under basic pH conditions compared with that at 293 K. Crystallization trials yielded three crystal forms from different temperature and pH conditions. Form I crystals (space group P2

Indexed as

Amino Acid SequenceArchaeal ProteinsBinding SitesCarbon-Oxygen LyasesChemical PrecipitationCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGlycolsHot TemperatureHydrogen-Ion ConcentrationKineticsModels, MolecularPlasmidsPolyethylene GlycolsArchaeal ProteinsCarbon-Oxygen LyasesGlycolshexylene glycolO-succinylhomoserine (thiol)-lyasepolyethylene glycol 3350Polyethylene GlycolsPyridoxal PhosphateRecombinant Proteinscystathionine γ-synthasehyperthermophilic enzymemethionine biosynthesispyridoxal 5′-phosphateSulfolobus tokodaiitranssulfuration

Identifiers

PMID28291751
PMCPMC5349309
OpenAlexW2591501087

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.