2fpr
Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.
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OverviewOverview
HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth, and eighth steps of l-histidine biosynthesis. The N-terminal domain, (HisB-N) possesses histidinol phosphate phosphatase activity, and its, crystal structure shows a single domain with fold similarity to the, haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the, crystal and in solution. The structure shows the presence of a structural, Zn(2+) ion stabilizing the conformation of an extended loop. Two metal, binding sites were also identified in the active site. Their presence was, further confirmed by isothermal titration calorimetry. HisB-N is active in, the presence of Mg(2+), Mn(2+), Co(2+), or Zn(2+), but Ca(2+) has an, inhibitory effect. We have determined structures of several intermediate, states corresponding to snapshots along the reaction pathway, including, that of the phosphoaspartate intermediate. A catalytic mechanism, different from that described for other HAD enzymes, is proposed requiring, the presence of the second metal ion not found in the active sites of, previously characterized HAD enzymes, to complete the second, half-reaction. The proposed mechanism is reminiscent of two-Mg(2+) ion, catalysis utilized by DNA and RNA polymerases and many nucleases. The, structure also provides an explanation for the inhibitory effect of, Ca(2+).
About this StructureAbout this Structure
2FPR is a Single protein structure of sequence from Escherichia coli with ZN, MG, NA and BR as ligands. Active as Histidinol-phosphatase, with EC number 3.1.3.15 Full crystallographic information is available from OCA.
ReferenceReference
Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway., Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M, J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:16966333
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