Evidence map›Paper›PMID 36748339›Full record

ArticleActa crystallographica. Section F, Structural biology communications2023

Structure of pyridoxal 5'-phosphate-bound D-threonine aldolase from Chlamydomonas reinhardtii.

Yuki Hirato, Masaru Goto, Taichi Mizobuchi, Hisashi Muramatsu, Minoru Tanigawa, Katsushi Nishimura

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

Article in Acta crystallographica. Section F, Structural biology communications, 2023. 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
0.1field-weighted citation impact, top 69% 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

6 authors at 3 institutions in 1 country.

Yuki HiratoDepartment of Biomolecular Science, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Masaru GotoDepartment of Biomolecular Science, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.ORCID 0000-0002-9317-0521
Taichi MizobuchiDepartment of Biomolecular Science, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Hisashi MuramatsuMultidisciplinary Science Cluster, Research and Education Faculty, Kochi University, B200 Monobe, Nankoku, Kochi 783-8502, Japan.
Minoru TanigawaDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Building No. 2, 1-5-1 Kanda Surugadai, Chiyoda, Tokyo 101-0062, Japan.
Katsushi NishimuraDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Building No. 2, 1-5-1 Kanda Surugadai, Chiyoda, Tokyo 101-0062, Japan.ORCID 0000-0002-3410-4698
Toho University · JPNihon University · JPKōchi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

D-Threonine aldolase (DTA) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes the reversible aldol reaction of glycine with a corresponding aldehyde to yield the D-form β-hydroxy-α-amino acid. This study produced and investigated the crystal structure of DTA from Chlamydomonas reinhardtii (CrDTA) at 1.85 Å resolution. To our knowledge, this is the first report on the crystal structure of eukaryotic DTA. Compared with the structure of bacterial DTA, CrDTA has a similar arrangement of active-site residues. On the other hand, we speculated that some non-conserved residues alter the affinity for substrates and inhibitors. The structure of CrDTA could provide insights into the structural framework for structure-guided protein engineering studies to modify reaction selectivity.

Indexed as

Chlamydomonas reinhardtiiAldehyde-LyasesCrystallography, X-RayGlycine HydroxymethyltransferasePhosphatesPyridoxal PhosphateSubstrate SpecificityAldehyde-LyasesGlycine HydroxymethyltransferasePhosphatesPyridoxal Phosphatethreonine acetaldehyde-lyaseChlamydomonas reinhardtiid-amino acidsd-threonine aldolasepyridoxal 5′-phosphate

Identifiers

PMID36748339
PMCPMC9903138
OpenAlexW4318984789

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.