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Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.
Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
Oxidative phosphorylation at the fin de siècle.
- M. Saraste
- Chemistry, BiologyScience
- 5 March 1999
Important new mechanistic insights into oxidative phosphorylation have emerged from recent three-dimensional structural analyses of ATP synthase and two of the respiratory enzyme complexes, cy tochrome bc1 and cytochrome c oxidase.
The P-loop--a common motif in ATP- and GTP-binding proteins.
Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles.
- M. Rief, J. Pascual, M. Saraste, H. Gaub
- Biology, PhysicsJournal of molecular biology
- 19 February 1999
The measured force required to mechanically unfold spectrin repeats shows that the forces stabilizing the coiled-coil lead to a mechanically much weaker structure than multiple hydrogen-bonded beta-sheets.
Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate.
Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen.
It is proposed that aerobic metabolism in organisms with cytochrome oxidase has a monophyletic and ancient origin, prior to the appearance of eubacterial oxygenic photosynthetic organisms.
Crystal structure of the SH3 domain in human Fyn; comparison of the three‐dimensional structures of SH3 domains in tyrosine kinases and spectrin.
The comparison between the crystal structures of Fyn and spectrin SH3 domains shows that a conserved surface patch, consisting mainly of aromatic residues, is flanked by two hairpin‐like loops which could modulate the binding properties of the aromatic surface.
Crystal structure of a Src-homology 3 (SH3) domain
The three-dimensional struc-ture at 1.8 Å resolution of the SH3 domain of the cytoskeletal protein spectrin expressed in Escherichia coli is reported and it is suggested that a protein ligand binds to this conserved surface of SH3.
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
The structure of the WW domain differs from that of the SH3 domain and reveals a new design for a protein module that uses stacked aromatic surface residues to arrange a binding site for proline-rich peptides.