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Cellular function and molecular structure of ecto-nucleotidases
The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions. Expand
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures.
All three structures reported herein support a mechanism of phosphate ester hydrolysis involving interaction of the substrate with Zn(II) followed by a nucleophilic attack on the phosphorus by an Fe(III)-coordinated hydroxide ion. Expand
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.
The active-site structure of the homodimeric 111-kilodalton KBPAP is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion. Expand
Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans.
Amylomaltase shows a similar arrangement of the catalytic side-chains as in previously characterized members of the alpha-amylase superfamily, indicating similar mechanisms of the glycosyl transfer reaction. Expand
Crystal structure of the plasmid maintenance system ɛ/ζ: Functional mechanism of toxin ζ and inactivation by ɛ2ζ2 complex formation
This work reports the first prokaryotic postsegregational killing system that has been entirely structurally characterized, and shows that free ζ acts as phosphotransferase by using ATP/GTP. Expand
Ecto-5’-nucleotidase: Structure function relationships
  • N. Sträter
  • Biology, Medicine
  • Purinergic Signalling
  • 16 May 2006
The currently available structural information on ecto-5’NT is reviewed in relation to the catalytic properties and enzyme function. Expand
Crystal Structure of Thermotoga maritima α-Glucosidase AglA Defines a New Clan of NAD+-dependent Glycosidases*
Glycoside hydrolase family 4 represents an unusual group of glucosidases with a requirement for NAD+, divalent metal cations, and reducing conditions. The family is also unique in its inclusion ofExpand
Insect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome.
Both apidaecins and oncocins were shown to bind with nanomolar dissociation constants to the 70S ribosome, and the chaperone DnaK is most likely not the main target of PrAMPs but it binds them with lower affinity. Expand
Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling.
Crystal structures of the dimeric human e5NT reveal an extensive 114° conformational switch between the open and closed forms of the enzyme, which indicates that structural control of the domain movement determines the selectivity for monophosphate nucleotides. Expand
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined and structure-based sequence comparisons show that the structure provides a model for animal 5'-NTs, which together with other ecton nucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system. Expand