Article

Two Glu/Asp Residues Cooperatively Mediate an Early Step of ATP Hydrolysis in GHKL ATPases MutL and GyrB

2026-04-01

Abstract excerpt

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...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: e4d9d7ef-afda-5ea2-b2f8-03f67e9dabd7
DOI: 10.64898/2026.03.31.715682

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Two Glu/Asp Residues Cooperatively Mediate an Early Step of ATP Hydrolysis in GHKL ATPases MutL and GyrBDOI 10.64898/2026.03.31.715682Read

Monovalent cation dependence and preference of GHKL ATPases and kinases.Semantic proximity Read

Conservation of functional asymmetry in the mammalian MutLα ATPase.Semantic proximity Read

Identification of general acid catalyst for the ATPase activity of Lynch syndrome-related MutL homologsSemantic proximity Read

A Lynch syndrome-associated mutation at a Bergerat ATP-binding fold destabilizes the structure of the DNA mismatch repair endonuclease MutL.Semantic proximity Read

The alternating ATPase domains of MutS control DNA mismatch repair.Semantic proximity Read

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.Semantic proximity Read

Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.Semantic proximity Read

Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6.Semantic proximity Read

A novel allosteric site employs a conserved inhibition mechanism in human kidney-type glutaminase.Semantic proximity Read

A Superfamily of ATPases with Diverse Functions Containing Either Classical or Deviant ATP-binding MotifSemantic proximity Read

Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair.Semantic proximity Read

The rad50 signature motif: essential to ATP binding and biological function.Semantic proximity Read