A common topology of proteins catalyzing ATP‐triggered reactions
Open Access
- 6 February 1995
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 359 (1), 1-5
- https://doi.org/10.1016/0014-5793(94)01438-7
Abstract
A protein fold, six parallel β strands surrounding the central α helix, is likely to be a common structure in protein families known to have a typical set of nucleotide binding consensus sequenced motifs A and B and to catalyze ATP‐triggered reactions. According to this ATP‐triggered protein fold, the conserved Glu (or Asp), which acts as a general base to activate a water molecule for an in‐line attack of the γ‐phosphate, is at the exit of the second β strand. The fifth β strand may be involved in propagation of conformational change triggered by ATP hydrolysis.Keywords
This publication has 22 references indexed in Scilit:
- Structural model of the ATP‐binding domain of the F1‐β subunit based on analogy to the RecA proteinFEBS Letters, 1994
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Spatial precision of a catalytic carboxylate of F1‐ATPase β subunit probed by introducing different carboxylate‐containing side chainsFEBS Letters, 1994
- The 2.2 Å crystal structure of transducin-α complexed with GTPγSNature, 1993
- Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolutionJournal of Molecular Biology, 1992
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990
- Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexesBiochemical and Biophysical Research Communications, 1987
- NMR studies of the magnesium-ATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzymeBiochemistry, 1985
- Sequencing a protein by X-ray crystallographyJournal of Molecular Biology, 1978
- The Mitochondrial ATPaseEuropean Journal of Biochemistry, 1975