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References (27)
-
B. Matthews (1968)
Solvent content of protein crystals.Journal of molecular biology, 33 2
-
Collaborative Computational (1994)
The CCP4 suite: programs for protein crystallography.Acta crystallographica. Section D, Biological crystallography, 50 Pt 5
-
K. Battaile, J. Molin-Case, R. Paschke, Ming Wang, D. Bennett, J. Vockley, Jung‐Ja Kim (2002)
Crystal Structure of Rat Short Chain Acyl-CoA Dehydrogenase Complexed with Acetoacetyl-CoAThe Journal of Biological Chemistry, 277
-
S. Ghisla, C. Thorpe, V. Massey (1984)
Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase: evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride.Biochemistry, 23 14
-
M. Souri, T. Aoyama, G. Hoganson, T. Hashimoto (1998)
Very‐long‐chain acyl‐CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membraneFEBS Letters, 426
-
A. Mccoy, R. Grosse-Kunstleve, P. Adams, M. Winn, L. Storoni, R. Read (2007)
Phaser crystallographic softwareJournal of Applied Crystallography, 40
-
(1956)
Chemistry and Biochemistry of Flavoenzymes, edited by F -
A. Vagin, A. Teplyakov (1997)
MOLREP: an Automated Program for Molecular ReplacementJournal of Applied Crystallography, 30
-
W. Cardoso, D. Kotton (2008)
Figure 3 -
Z. Otwinowski, W. Minor (1997)
[20] Processing of X-ray diffraction data collected in oscillation mode.Methods in enzymology, 276
-
Y. Ikeda, K. Okamura-Ikeda, K. Tanaka (1985)
Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.The Journal of biological chemistry, 260 2
-
Jung‐Ja Kim, R. Miura (2004)
Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences.European journal of biochemistry, 271 3
-
R. McAndrew, Yudong Wang, A. Mohsen, M. He, J. Vockley, Jung‐Ja Kim (2008)
Structural Basis for Substrate Fatty Acyl Chain SpecificityJournal of Biological Chemistry, 283
-
R. Ensenauer, M. He, J. Willard, E. Goetzman, T. Corydon, B. Vandahl, A. Mohsen, G. Isaya, J. Vockley (2005)
Human Acyl-CoA Dehydrogenase-9 Plays a Novel Role in the Mitochondrial β-Oxidation of Unsaturated Fatty Acids*Journal of Biological Chemistry, 280
-
Jung-Ja Kim, Ming Wang, R. Paschke (1994)
Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.Proceedings of the National Academy of Sciences of the United States of America, 90 16
-
K. Tiffany, D. Roberts, Ming Wang, R. Paschke, A. Mohsen, Jerry Vockley, Jung-Ja Kim (1997)
Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.Biochemistry, 36 28
-
C. Thorpe, Jujng‐Ja Kim (1995)
Structure and mechanism of action of the Acyl‐CoA dehydrogenases 1The FASEB Journal, 9
-
Hyun-Joo Lee, Ming Wang, R. Paschke, Andreas Nandy, Sandro Ghisla, Jung-Ja Kim (1996)
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.Biochemistry, 35 38
-
K. Izai, Y. Uchida, T. Orii, S. Yamamoto, T. Hashimoto (1992)
Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase.The Journal of biological chemistry, 267 2
-
F. Ruzicka, H. Beinert (1977)
A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway.The Journal of biological chemistry, 252 23
-
A. Satoh, Y. Nakajima, I. Miyahara, K. Hirotsu, Takeyuki Tanaka, Y. Nishina, K. Shiga, H. Tamaoki, C. Setoyama, R. Miura (2003)
Structure of the transition state analog of medium-chain acyl-CoA dehydrogenase. Crystallographic and molecular orbital studies on the charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-thiaoctanoyl-CoA.Journal of biochemistry, 134 2
-
Jia Zhang, Weiping Zhang, D. Zou, Guoyou Chen, T. Wan, Minghui Zhang, Xuetao Cao (2002)
Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family.Biochemical and biophysical research communications, 297 4
-
Timothy Bowles, Audrey Metz, Jami O'Quin, Z. Wawrzak, B. Eichman (2008)
Structure and DNA binding of alkylation response protein AidBProceedings of the National Academy of Sciences, 105
-
E. Steyn-Parvé, H. Beinert (1956)
On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transferring flavoprotein.The Journal of biological chemistry, 218 2
-
(1994)
Flavins and Flavoproteins, edited by K -
Z. Fu, Ming Wang, R. Paschke, K. Rao, F. Frerman, Jung‐Ja Kim (2004)
Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions.Biochemistry, 43 30
-
Very-long-chain acyl-CoA dehydrogenase 429
- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2010
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309110005002
- pmid
- 20383014
- Publisher site
- See Article on Publisher Site
Abstract
Acyl‐CoA dehydrogenase (acyl‐CoA:(acceptor) 2,3‐oxidoreductase; EC 1.3.99.3) catalyzes the first reaction step in mitochondrial fatty‐acid β‐oxidation. Here, the very‐long‐chain acyl‐CoA dehydrogenase from Caenorhabditis elegans (cVLCAD) has been cloned and overexpressed in Escherichia coli strain BL21 (DE3). Interestingly, unlike other very‐long‐chain acyl‐CoA dehydrogenases, cVLCAD was found to form a tetramer by size‐exclusion chromatography coupled with in‐line static light‐scattering, refractive‐index and ultraviolet measurements. Purified cVLCAD (12 mg ml−1) was successfully crystallized by the hanging‐drop vapour‐diffusion method under conditions containing 100 mM Tris–HCl pH 8.0, 150 mM sodium chloride, 200 mM magnesium formate and 13% PEG 3350. The crystal has a tetragonal form and a complete diffraction data set was collected and processed to 1.8 Å resolution. The crystal belonged to space group C2, with unit‐cell parameters a = 138.6, b = 116.7, c = 115.3 Å, α = γ = 90.0, β = 124.0°. A self‐rotation function indicated the existence of one noncrystallographic twofold axis. A preliminary molecular‐replacement solution further confirmed the presence of two molecules in one asymmetric unit, which yields a Matthews coefficient VM of 2.76 Å3 Da−1 and a solvent content of 55%.
Journal
Acta Crystallographica Section F – Wiley
Published: Apr 1, 2010