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Title: Crystallization and preliminary crystallographic study of carnosinase CN2 from mice

Abstract

Mouse carnosinase was crystallized in complex with Zn{sup 2+} or Mn{sup 2+} and the complexes are undergoing structure determination by the MAD method. Mammalian tissues contain several histidine-containing dipeptides, of which l-carnosine is the best characterized and is found in various tissues including the brain and skeletal muscles. However, the mechanism for its biosynthesis and degradation have not yet been fully elucidated. Crystallographic study of carnosinase CN2 from mouse has been undertaken in order to understand its enzymatic mechanism from a structural viewpoint. CN2 was crystallized by the hanging-drop vapour-diffusion technique using PEG 3350 as a precipitant. Crystals were obtained in complex with either Mn{sup 2+} or Zn{sup 2+}. Both crystals of CN2 belong to the monoclinic space group P2{sub 1} and have almost identical unit-cell parameters (a = 54.41, b = 199.77, c = 55.49 Å, β = 118.52° for the Zn{sup 2+} complex crystals). Diffraction data were collected to 1.7 and 2.3 Å for Zn{sup 2+} and Mn{sup 2+} complex crystals, respectively, using synchrotron radiation. Structure determination is ongoing using the multiple-wavelength anomalous diffraction (MAD) method.

Authors:
; ; ; ; ; ; ;  [1]
  1. Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka 565-0871 (Japan)
Publication Date:
OSTI Identifier:
22356366
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 62; Journal Issue: Pt 10; Other Information: PMCID: PMC2225185; PMID: 17012794; PUBLISHER-ID: hc5005; OAI: oai:pubmedcentral.nih.gov:2225185; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; HISTIDINE; SPACE GROUPS; SYNCHROTRON RADIATION; WAVELENGTHS

Citation Formats

Yamashita, Tetsuo, Unno, Hideaki, Ujita, Sayuri, Otani, Hiroto, Okumura, Nobuaki, Hashida-Okumura, Akiko, Nagai, Katsuya, and Kusunoki, Masami. Crystallization and preliminary crystallographic study of carnosinase CN2 from mice. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106034701.
Yamashita, Tetsuo, Unno, Hideaki, Ujita, Sayuri, Otani, Hiroto, Okumura, Nobuaki, Hashida-Okumura, Akiko, Nagai, Katsuya, & Kusunoki, Masami. Crystallization and preliminary crystallographic study of carnosinase CN2 from mice. United Kingdom. https://doi.org/10.1107/S1744309106034701
Yamashita, Tetsuo, Unno, Hideaki, Ujita, Sayuri, Otani, Hiroto, Okumura, Nobuaki, Hashida-Okumura, Akiko, Nagai, Katsuya, and Kusunoki, Masami. 2006. "Crystallization and preliminary crystallographic study of carnosinase CN2 from mice". United Kingdom. https://doi.org/10.1107/S1744309106034701.
@article{osti_22356366,
title = {Crystallization and preliminary crystallographic study of carnosinase CN2 from mice},
author = {Yamashita, Tetsuo and Unno, Hideaki and Ujita, Sayuri and Otani, Hiroto and Okumura, Nobuaki and Hashida-Okumura, Akiko and Nagai, Katsuya and Kusunoki, Masami},
abstractNote = {Mouse carnosinase was crystallized in complex with Zn{sup 2+} or Mn{sup 2+} and the complexes are undergoing structure determination by the MAD method. Mammalian tissues contain several histidine-containing dipeptides, of which l-carnosine is the best characterized and is found in various tissues including the brain and skeletal muscles. However, the mechanism for its biosynthesis and degradation have not yet been fully elucidated. Crystallographic study of carnosinase CN2 from mouse has been undertaken in order to understand its enzymatic mechanism from a structural viewpoint. CN2 was crystallized by the hanging-drop vapour-diffusion technique using PEG 3350 as a precipitant. Crystals were obtained in complex with either Mn{sup 2+} or Zn{sup 2+}. Both crystals of CN2 belong to the monoclinic space group P2{sub 1} and have almost identical unit-cell parameters (a = 54.41, b = 199.77, c = 55.49 Å, β = 118.52° for the Zn{sup 2+} complex crystals). Diffraction data were collected to 1.7 and 2.3 Å for Zn{sup 2+} and Mn{sup 2+} complex crystals, respectively, using synchrotron radiation. Structure determination is ongoing using the multiple-wavelength anomalous diffraction (MAD) method.},
doi = {10.1107/S1744309106034701},
url = {https://www.osti.gov/biblio/22356366}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 10,
volume = 62,
place = {United Kingdom},
year = {Sun Oct 01 00:00:00 EDT 2006},
month = {Sun Oct 01 00:00:00 EDT 2006}
}