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Three-dimensional structure of myosin subfragment-1: a molecular motor.
The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described, and this structure of a molecular motor was determined by single crystal x-ray diffraction. Expand
Structure of the actin-myosin complex and its implications for muscle contraction.
The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies. Expand
Three-dimensional structure of the Tn5 synaptic complex transposition intermediate.
The three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn 5 transposon end DNA determined to 2.3 angstrom resolution is reported, which provides a molecular framework for understanding many aspects of transposition, including the binding of transpos on end DNA by one subunit and cleavage by a second. Expand
Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle
It is suggested that the mutations associated with the identification of distinct missense mutations in a skeletal/ventricular ELC and RLC are associated with a rare variant of cardiac hypertrophy as well as abnormal skeletal muscle. Expand
Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism*
Recent advances in the understanding of the structure and function of the Leloir pathway are presented, highlighting their important metabolic role in normal galactose metabolism. Expand
X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myOSin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported, indicating that myos in undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosIn motor domain. Expand
Structure, mechanism and regulation of pyruvate carboxylase.
- S. Jitrapakdee, M. St. Maurice, I. Rayment, W. Cleland, J. Wallace, P. Attwood
- Biology, Medicine
- The Biochemical journal
- 1 August 2008
The first cloning of the promoter of the PC gene in mammals and subsequent transcriptional studies reveal some key cognate transcription factors regulating tissue-specific expression, which offers some prospects for the study of this important enzyme. Expand
The structural basis of blebbistatin inhibition and specificity for myosin II
- J. Allingham, Robert Smith, I. Rayment
- Biology, Medicine
- Nature Structural &Molecular Biology
- 6 March 2005
The structure of blebbistatin, which inhibits specific myosin isoforms, bound to the motor domain of Dictyostelium discoideum myOSin II is reported, which reveals the structural basis for its specificity and provides insight into the development of new agents. Expand
The 1.5-Å Resolution Crystal Structure of Bacterial Luciferase in Low Salt Conditions*
- A. Fisher, T. B. Thompson, J. Thoden, T. O. Baldwin, I. Rayment
- Biology, Medicine
- The Journal of Biological Chemistry
- 6 September 1996
The structure presented here will furnish a detailed molecular model for all bacterial luciferases and suggests that the structural similarities between luciferase and a nonfluorescent flavoprotein suggest that the two proteins originated from a common ancestor. Expand
Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product.
- J. Thoden, H. Holden, G. Wesenberg, F. Raushel, I. Rayment
- Chemistry, Medicine
- 27 May 1997
The two halves of the large subunit are related by a nearly exact 2-fold rotational axis, thus suggesting that this polypeptide chain evolved from a homodimeric precursor. Expand