Evidence map›Paper›PMID 42788712›Full record

ArticleeLife2026

Two Glu/Asp residues cooperatively mediate an early step of ATP hydrolysis in GHKL ATPases MutL and GyrB.

Kenji Fukui, Ayaka Shibuya, Takeshi Murakawa, Takato Yano

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2026. 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
–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

0 citing papers in PubMed.

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

4 authors.

Kenji FukuiDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, Takatsuki, Japan.ORCID https://orcid.org/0000-0003-2463-7578
Ayaka ShibuyaDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, Takatsuki, Japan.
Takeshi MurakawaDepartment of Chemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, Takatsuki, Japan.ORCID https://orcid.org/0000-0001-5905-532X
Takato YanoDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, Takatsuki, Japan.

Funding

Japan Society for the Promotion of Science Grant-in-Aid for Scientific Research (C) (Basic Section 38030: Applied biochemistry) 24K08718
6 · The paper itself

Abstract

GHKL ATPases share a unique Bergerat ATP-binding fold and regulate diverse biological processes through ATP-dependent conformational changes. An early step of ATP hydrolysis in this family has been attributed to a single highly conserved glutamate residue proposed to function as the general base. However, mutations of this residue impair both the ATPase activity and ATP binding, complicating interpretation of its catalytic role. Re-examination of the high-resolution crystal structures revealed a second conserved acidic residue positioned within a hydrogen-bonding distance from the nucleophilic water molecule. Using

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAspartic AcidBacterial ProteinsDNA GyraseGlutamic AcidAquifexCrystallography, X-RayHydrolysisModels, MolecularProtein ConformationAdenosine TriphosphatasesAdenosine TriphosphateAspartic AcidBacterial ProteinsDNA GyraseGlutamic AcidAquifex aeolicusGHKL ATPaseGyrBhumanmolecular biophysicsMutLstructural biologyX-ray crystallography

Identifiers

PMID42788712
PMCPMC13614785

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.