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Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism*
TLDR
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-.
TLDR
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
Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
TLDR
From the three-dimensional structures of the enzyme-bound substrate and product, it has been possible to propose a unique catalytic mechanism for dihydroorotase, and strikingly, in subunit II, carbamoyl L-aspartate is observed binding near the binuclear metal center with its carboxylate side chain ligating the two metals and thus displacing the bridging hydroxide ion. Expand
The 1.5-Å Resolution Crystal Structure of Bacterial Luciferase in Low Salt Conditions*
TLDR
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.
TLDR
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
Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli.
TLDR
It is concluded that Tyr 149 provides the driving force for general acid-base catalysis, with Ser 124 playing an important role in mediating proton transfer. Expand
Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
TLDR
This investigation reveals for the first time that a conserved tyrosine, namely Tyr 157, is in the proper position to interact directly with the 4'-hydroxyl group of the sugar substrate and to thus serve as the active-site base in the resting state of human epimerase. Expand
X-ray Structures of the Apo and MgATP-bound States ofDictyostelium discoideum Myosin Motor Domain*
TLDR
The crystallized protein is enzymatically active in solution, indicating that the conformation of myosin observed in chicken skeletal myosIn subfragment-1 is unable to hydrolyze ATP and most likely represents the pre-hydrolysis structure for the myOSin head that occurs after release from actin. Expand
Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding*
TLDR
The three-dimensional structure of the E. coli biotin carboxylase complexed with ATP is described and it is demonstrated that the protein belongs to the ATP-grasp superfamily. Expand
Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
TLDR
The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that seen for GMP synthet enzyme. Expand
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