GHKL, an emergent ATPase/kinase superfamily.

By Rinku Dutta, Masayori Inouye. TIBS -Trends in Biochemical Sciences. Regular ed, 2000

773 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/f11a2c3677b34ce75ac2738cd80f2d3db377421b

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Citations in the corpus

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. (2005, background): “Its structure has been solved for the yeast (Prodromou et al., 1997) and human (Stebbins et al., 1997) isoforms and contains a unique ATP binding site, termed the Bergerat fold, found in a growing superfamily of proteins (Dutta and Inouye, 2000).”
Hsp90 as a capacitor of phenotypic variation (2002, background): “The drugs geldanamycin (GDA) and radicicol are structurally unrelated; however, each inhibits Hsp90 function through multiple, distinct contacts with residues in its highly unusual, evolutionarily conserved nucleotide-binding pocke”
The multifaceted mismatch-repair system (2006, background): “MutL homologues: molecular matchmakers? The MutL proteins are ATPases of the GHKL (gyrase/Hsp90/histidine-kinase/MutL) famil”
Light signal transduction in higher plants. (2004, background): “The carboxy-terminal half of phytochrome contains two subdomains: a PAS-related domain (PRD) containing two PAS domains (PAS-A and PAS-B) (11) and a histidine kinase-related domain (HKRD), which belongs to the ATPase/kinase GHKL (gyrase, Hsp90, histidine kinase, MutL) superfamily (Figure 3A) (42, 13”
The Evolution of Two-Component Signal Transduction Systems (2012, background): “However, one clue is that histidine kinases share distant homology in their ATP-binding domains with Hsp90, the mismatch repair protein MutL, and type II topoisomerases (17, 18).”
Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1 (2003, background): “However, beyond this region, there are residues that are thought to interact with the phosphate of ATP during ATP hydrolysis, as has been shown for other members of the GHKL family (201, 209, 210).”
Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis (2012, background): “The catalytic region of these proteins consists of a conserved cytoplasmic two-domain catalytic core, which features a homodimeric four-helix bundle harboring the site of phosphorylation, the HisKA domain, and an ATP-binding domain recognized by the HATPase_c Hidden Markov model (HMM) shared by vari”
HSP90 and the chaperoning of cancer (2005, background): “The N-terminal domain contains an unusual adenine-nucleotide-binding pocket known as the Bergerat fol”
Genetic regulation of biological nitrogen fixation (2004, background): “vinelandii NifL contains a HATPase_c domain and belongs to the superfamily of GHKL (gyrase, Hsp90, histidine kinase, mutL) ATP-ases, which includes the histidine protein kinases, DNA gyrase and Hsp90 (Ref”
Hsp90: a specialized but essential protein-folding tool. (2001, background): “The ATP-binding domain of Hsp90 is structurally related to a superfamily of homodimeric ATPases, comprising in addition to Hsp90 DNA gyrase and topoisomerase II, the DNA mismatch repair protein MutL, and the histidine kinases CheA and EnvZ (Bergerat et al., 1997; Dutta and Inouye, 2000).”
Biological Insights from Structures of Two-Component Proteins (2009, background): “The α/β sandwich fold of the CA domain (Figure 2a) is distinct from any known Ser/Thr/Tyr kinases but similar to the ATPase domains of the GHL ATPase superfamily, whose members include GyrB, Hsp90, and MutL (30).”