Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23

J Struct Biol. 1999 Jun 1;126(1):80-3. doi: 10.1006/jsbi.1999.4088.

Abstract

HBP-23 is a stress-induced multifunctional rat protein that belongs to a novel family of antioxidant proteins, referred to as peroxiredoxins, and exhibits heme-binding and inhibition of c-Abl protein tyrosine kinase. Recombinant HBP-23 was crystallized by a hanging-drop vapor-diffusion method. The crystals belong to space group P41212 or P43212 with unit-cell dimensions of a = b = 73.47 A, c = 210.37 A and contain two protein molecules in the asymmetric unit. A data set at 2.7-A resolution was collected with a cryo-crystallographic technique. Crystals of selenomethionyl HBP-23 were also obtained under the same conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray / methods
  • Escherichia coli
  • Heme-Binding Proteins
  • Hemeproteins / biosynthesis
  • Hemeproteins / chemistry*
  • Hemeproteins / isolation & purification
  • Rats
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Carrier Proteins
  • Heme-Binding Proteins
  • Hemeproteins
  • Recombinant Proteins