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Title: Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus

Abstract

To elucidate the mechanism of regulation of aspartate kinase, the regulatory subunit (the β subunit of T. thermophilus aspartate kinase) was crystallized in the presence of the inhibitor threonine. Aspartate kinase (AK) from Thermus thermophilus, which catalyzes the first step of threonine and methionine biosynthesis, is regulated via feedback inhibition by the end product threonine. To elucidate the mechanism of regulation of AK, the regulatory subunit (the β subunit of T. thermophilus AK) was crystallized in the presence of the inhibitor threonine. Diffraction data were collected to 2.15 Å at a synchrotron source. The crystal belongs to the cubic space group P4{sub 3}32 or P4{sub 1}32, with unit-cell parameters a = b = c = 141.8 Å.

Authors:
; ;  [1];  [1];  [2]
  1. Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657 (Japan)
  2. (Japan)
Publication Date:
OSTI Identifier:
22360262
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 2; Other Information: PMCID: PMC2330127; PMID: 17277448; PUBLISHER-ID: gx5106; OAI: oai:pubmedcentral.nih.gov:2330127; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; FEEDBACK; SPACE GROUPS

Citation Formats

Yoshida, Ayako, Tomita, Takeo, Kuzuyama, Tomohisa, Nishiyama, Makoto, E-mail: umanis@mail.ecc.u-tokyo.ac.jp, and RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148. Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106055837.
Yoshida, Ayako, Tomita, Takeo, Kuzuyama, Tomohisa, Nishiyama, Makoto, E-mail: umanis@mail.ecc.u-tokyo.ac.jp, & RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148. Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus. United Kingdom. doi:10.1107/S1744309106055837.
Yoshida, Ayako, Tomita, Takeo, Kuzuyama, Tomohisa, Nishiyama, Makoto, E-mail: umanis@mail.ecc.u-tokyo.ac.jp, and RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148. Thu . "Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus". United Kingdom. doi:10.1107/S1744309106055837.
@article{osti_22360262,
title = {Purification, crystallization and preliminary X-ray analysis of the regulatory subunit of aspartate kinase from Thermus thermophilus},
author = {Yoshida, Ayako and Tomita, Takeo and Kuzuyama, Tomohisa and Nishiyama, Makoto, E-mail: umanis@mail.ecc.u-tokyo.ac.jp and RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148},
abstractNote = {To elucidate the mechanism of regulation of aspartate kinase, the regulatory subunit (the β subunit of T. thermophilus aspartate kinase) was crystallized in the presence of the inhibitor threonine. Aspartate kinase (AK) from Thermus thermophilus, which catalyzes the first step of threonine and methionine biosynthesis, is regulated via feedback inhibition by the end product threonine. To elucidate the mechanism of regulation of AK, the regulatory subunit (the β subunit of T. thermophilus AK) was crystallized in the presence of the inhibitor threonine. Diffraction data were collected to 2.15 Å at a synchrotron source. The crystal belongs to the cubic space group P4{sub 3}32 or P4{sub 1}32, with unit-cell parameters a = b = c = 141.8 Å.},
doi = {10.1107/S1744309106055837},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 63,
place = {United Kingdom},
year = {Thu Feb 01 00:00:00 EST 2007},
month = {Thu Feb 01 00:00:00 EST 2007}
}