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Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23.
J Struct Biol. 1999 Jun 01; 126(1):80-3.JS

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.

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Authors+Show Affiliations

Hirotsu S
Department of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Nara, Ikoma, 630-01, Japan.
Abe Y
No affiliation info available
Nagahara N
No affiliation info available
Hori H
No affiliation info available
Nishino T
No affiliation info available
Okada K
No affiliation info available
Hakoshima T
No affiliation info available

MeSH

AnimalsCarrier ProteinsCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliHeme-Binding ProteinsHemeproteinsRatsRecombinant Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10329492

Citation

Hirotsu, S, et al. "Crystallographic Characterization of a Stress-induced Multifunctional Protein, Rat HBP-23." Journal of Structural Biology, vol. 126, no. 1, 1999, pp. 80-3.
Hirotsu S, Abe Y, Nagahara N, et al. Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23. J Struct Biol. 1999;126(1):80-3.
Hirotsu, S., Abe, Y., Nagahara, N., Hori, H., Nishino, T., Okada, K., & Hakoshima, T. (1999). Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23. Journal of Structural Biology, 126(1), 80-3.
Hirotsu S, et al. Crystallographic Characterization of a Stress-induced Multifunctional Protein, Rat HBP-23. J Struct Biol. 1999 Jun 1;126(1):80-3. PubMed PMID: 10329492.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallographic characterization of a stress-induced multifunctional protein, rat HBP-23. AU - Hirotsu,S, AU - Abe,Y, AU - Nagahara,N, AU - Hori,H, AU - Nishino,T, AU - Okada,K, AU - Hakoshima,T, PY - 1999/5/18/pubmed PY - 1999/5/18/medline PY - 1999/5/18/entrez SP - 80 EP - 3 JF - Journal of structural biology JO - J Struct Biol VL - 126 IS - 1 N2 - 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. SN - 1047-8477 UR - https://www.unboundmedicine.com/medline/citation/10329492/Crystallographic_characterization_of_a_stress_induced_multifunctional_protein_rat_HBP_23_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1047-8477(99)94088-1 DB - PRIME DP - Unbound Medicine ER -