Evidence map›Paper›PMID 40864147›Full record

ArticleActa crystallographica. Section F, Structural biology communications2025

Crystal structure of a seven-substitution mutant of hydroxynitrile lyase from rubber tree.

Colin T Pierce, Lauren R Greenberg, Meghan E Walsh, Ke Shi, Drenen J Magee, Hideki Aihara, Wendy Gordon, Robert L Evans, Romas J Kazlauskas

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2025. 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
–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

1 citing paper in PubMed.

  1. 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

9 authors.

Colin T PierceDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Lauren R GreenbergDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.ORCID 0000-0001-6602-2067
Meghan E WalshDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Ke ShiDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Drenen J MageeCrown College, Saint Bonifacius, Minnesota, USA.ORCID 0009-0009-7725-618X
Hideki AiharaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.ORCID 0000-0001-7508-6230
Wendy GordonDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Robert L EvansDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.
Romas J KazlauskasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.ORCID 0000-0002-3570-2411

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Structural studies of viral replication and invasionR35GM118047 · NIGMS · UNIVERSITY OF MINNESOTA · PI Hideki Aihara · 2016 to 2026
$6.3M
Mechanism and modulation of Amyloid Precursor Protein proteolysisR35GM119483 · NIGMS · UNIVERSITY OF MINNESOTA · PI WENDY RYAN GORDON · 2016 to 2026
$4.6M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
National Science Foundation CBET-2039039NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM118047NIGMS NIH HHS R35 GM119483NIH HHS P30 GM124165NIH HHS R35 GM118047NIH HHS R35 GM119483NIH HHS S10 RR029205Office of Fossil Energy, Office of Science DE-AC02-06CH11357
6 · The paper itself

Abstract

The α/β-hydrolase fold superfamily includes esterases and hydroxynitrile lyases which, despite catalyzing different reactions, share a Ser-His-Asp catalytic triad. We report a 1.99 Å resolution crystal structure of HNL6V, an engineered variant of hydroxynitrile lyase from Hevea brasiliensis (HbHNL) containing seven amino-acid substitutions (T11G, E79H, C81L, H103V, N104A, G176S and K236M). The structure reveals that HNL6V maintains the characteristic α/β-hydrolase fold while exhibiting systematic shifts in backbone and catalytic atom positions. Compared with wild-type HbHNL, the C

Indexed as

Aldehyde-LyasesHeveaPlant ProteinsAmino Acid SequenceAmino Acid SubstitutionCatalytic DomainCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionModels, MolecularMutationRecombinant ProteinsAldehyde-Lyasesmandelonitrile lyasePlant ProteinsRecombinant Proteinsengineered proteinsesteraseshydroxynitrile lyasesα/β-hydrolase fold

Identifiers

PMID40864147
PMCPMC12400193

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.