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Title: Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae

Abstract

Enoyl-acyl carrier protein (ACP) reductases are responsible for bacterial type II fatty-acid biosynthesis and are attractive targets for developing novel antibiotics. The S. pneumoniae enoyl-ACP reductase (FabK) was crystallized and selenomethionine MAD data were collected to 2 Å resolution. The enoyl-acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty-acid biosynthesis. Selenomethionine-substituted FabK was purified and crystallized by the hanging-drop vapour-diffusion method at 277 K. The crystal belongs to space group P2{sub 1}, with unit-cell parameters a = 50.26, b = 126.70, c = 53.63 Å, β = 112.46°. Diffraction data were collected to 2.00 Å resolution using synchrotron beamline BL32B2 at SPring-8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.

Authors:
; ; ; ;  [1]
  1. Pharmaceutical Research Center, Meiji Seika Kaisha Ltd, 760 Morooka-cho, Kohoku-ku, Yokohama 222-8567 (Japan)
Publication Date:
OSTI Identifier:
22360233
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 62; Journal Issue: Pt 6; Other Information: PMCID: PMC2243098; PMID: 16754986; PUBLISHER-ID: ll5063; OAI: oai:pubmedcentral.nih.gov:2243098; 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; CARBOXYLIC ACIDS; CARRIERS; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; ELONGATION; MOLECULES; RESOLUTION; SOLVENTS; SPACE GROUPS; SYNCHROTRONS

Citation Formats

Saito, Jun, Yamada, Mototsugu, Watanabe, Takashi, Kitagawa, Hideo, and Takeuchi, Yasuo. Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106017039.
Saito, Jun, Yamada, Mototsugu, Watanabe, Takashi, Kitagawa, Hideo, & Takeuchi, Yasuo. Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae. United Kingdom. https://doi.org/10.1107/S1744309106017039
Saito, Jun, Yamada, Mototsugu, Watanabe, Takashi, Kitagawa, Hideo, and Takeuchi, Yasuo. 2006. "Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae". United Kingdom. https://doi.org/10.1107/S1744309106017039.
@article{osti_22360233,
title = {Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae},
author = {Saito, Jun and Yamada, Mototsugu and Watanabe, Takashi and Kitagawa, Hideo and Takeuchi, Yasuo},
abstractNote = {Enoyl-acyl carrier protein (ACP) reductases are responsible for bacterial type II fatty-acid biosynthesis and are attractive targets for developing novel antibiotics. The S. pneumoniae enoyl-ACP reductase (FabK) was crystallized and selenomethionine MAD data were collected to 2 Å resolution. The enoyl-acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty-acid biosynthesis. Selenomethionine-substituted FabK was purified and crystallized by the hanging-drop vapour-diffusion method at 277 K. The crystal belongs to space group P2{sub 1}, with unit-cell parameters a = 50.26, b = 126.70, c = 53.63 Å, β = 112.46°. Diffraction data were collected to 2.00 Å resolution using synchrotron beamline BL32B2 at SPring-8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.},
doi = {10.1107/S1744309106017039},
url = {https://www.osti.gov/biblio/22360233}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 6,
volume = 62,
place = {United Kingdom},
year = {Thu Jun 01 00:00:00 EDT 2006},
month = {Thu Jun 01 00:00:00 EDT 2006}
}