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Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation.
It is suggested that the translocation domain in other BoNTs follows a two-step process to attain translocation-competent conformation as in BoNT E, and this is a probable reason for its faster toxic rate compared to BoNT A. Expand
Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi
The surface of OspC that would project away from the spirochete's membrane has a region of strong negative electrostatic potential which may be involved in binding to positively charged host ligands. Expand
Crystal structure of a putative CN hydrolase from yeast
Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. Expand
Crystal structure of trehalose‐6‐phosphate phosphatase–related protein: Biochemical and biological implications
We report here the crystal structure of a trehalose‐6‐phosphate phosphatase–related protein (T6PP) from Thermoplasma acidophilum, TA1209, determined by the dual‐wavelength anomalous diffraction (DAD)Expand
Substrate Binding Mode and Its Implication on Drug Design for Botulinum Neurotoxin A
The crystal structures of the catalytic domain of BoNT/A with its uncleavable SNAP-25 peptide and its variant 197RRATKM202 to 1.5 Å and 1.6 Å are reported, which should form the basis for design of potent inhibitors for this neurotoxin. Expand
Structural genomics of protein phosphatases
The New York SGX Research Center for Structural Genomics has determined structures of 21 distinct protein phosphatases, providing insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. Expand
Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway.
The structural differences responsible for the loss of activity of the mutant provide a common model for the catalytic pathway of Clostridium neurotoxins since Glu212 is conserved and has a similar role in all serotypes. Expand
A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa
The crystal structure of HEX-1 is solved at 1.8 Å, which provides the structural basis of its self-assembly and reveals the existence of three intermolecular interfaces that promote the formation of a three-dimensional protein lattice. Expand
Structure- and Substrate-based Inhibitor Design for Clostridium botulinum Neurotoxin Serotype A*
Crystal structures of botulinum neurotoxin type A catalytic domain in complex with four inhibitory substrate analog tetrapeptides show for the first time the interactions between the substrate and enzyme at the active site and delineate residues important for substrate stabilization and catalytic activity. Expand
Role of metals in the biological activity of Clostridium botulinum neurotoxins.
The crystal structures of botulinum neurotoxin type B at various pHs and of an apo form of the neurotoxin are reported, and the role of metal ions and the effect of pH variation in the biological activity are discussed. Expand