Evidence map›Paper›PMID 36054591›Full record

ArticleFEBS open bio2022

Functional analysis of the N-terminal region of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.

Kohei Sasamoto, Tomoki Himiyama, Kunihiko Moriyoshi, Takashi Ohmoto, Koichi Uegaki, Tsutomu Nakamura, Yoshiaki Nishiya

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

Article in FEBS open bio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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 at 4 institutions in 1 country.

Kohei SasamotoDivision of Life Science, Graduate School of Science and Engineering, Setsunan University, Osaka, Japan.ORCID 0000-0001-6005-7939
Tomoki HimiyamaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Osaka, Japan.ORCID 0000-0001-5252-1834
Kunihiko MoriyoshiOsaka Research Institute of Industrial Science and Technology, Japan.
Takashi OhmotoOsaka Research Institute of Industrial Science and Technology, Japan.
Koichi UegakiDepartment of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan.ORCID 0000-0001-6659-2596
Tsutomu NakamuraBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Osaka, Japan.ORCID 0000-0002-5511-8087
Yoshiaki NishiyaDivision of Life Science, Graduate School of Science and Engineering, Setsunan University, Osaka, Japan.
National Institute of Advanced Industrial Science and Technology · JPOsaka Research Institute of Industrial Science and Technology · JPSetsunan University · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866) has an N-terminal region (NTR; residues 23-135) between the signal sequence (residues 1-22) and the catalytic domain (residues 136-324), which is of unknown function. Our previous study revealed the crystal structure of the wild-type (WT) enzyme containing the NTR and the catalytic domain. Although the structure of the catalytic domain was successfully determined, that of the NTR was undetermined, as its electron density was unclear. In this study, we investigated the role of the NTR through functional and structural analyses of NTR truncation mutants. Based on sequence and secondary structure analyses, NTR was confirmed to be an intrinsically disordered region. The truncation of NTR significantly decreased the solubility of the proteins at low salt concentrations compared with that of the WT. The NTR-truncated mutant easily crystallized in a conventional buffer solution. The crystal exhibited crystallographic properties comparable with those of the WT crystals suitable for structural determination. These results suggest that NTR plays a role in maintaining the solubility and inhibiting the crystallization of the catalytic domain.

Indexed as

AcetylesteraseBacillotaProtein Sorting SignalsAcetylesteraseacetylxylan esteraseProtein Sorting Signalsacetylxylan esteraseCaldanaerobactercrystallizationintrinsically disordered regionprotein solubility

Identifiers

PMID36054591
PMCPMC9527590
OpenAlexW4293168865

What OpenQuestion holds

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LicenceCC BY
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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.