Abstract
During fatty-acid biosynthesis, enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the reduction of trans-2-enoyl-ACP to fully saturated acyl-ACP via the ubiquitous fatty-acid synthase system. NADH-dependent enoyl-ACP reductase (FabI) from Pseudomonas aeruginosa has been purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. Triclosan is an inhibitor of FabI and forms a stable ternary complex in the presence of NADH. The crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 Å, respectively. The crystals both belonged to space group P21, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 Å, Β = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 Å, Β = 116.162° for the complex. Preliminary molecular replacement further confirmed the presence of four tetramers of native FabI and one tetramer of the complex in the asymmetric unit, corresponding to Matthews coefficients (V M) of 2.46 and 2.05 Å 3 Da -1 and solvent contents of 50.1 and 40.1%, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 214-216 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 67 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2011 Feb 1 |
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Keywords
- Enoyl-acyl carrier protein reductases
- FabI
- Fatty-acid synthesis
- Pseudomonas aeruginosa
- Triclosan
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Structural Biology
- Genetics
- Condensed Matter Physics
Cite this
Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Psuedomonas aeruginosa. / Lee, Jeong Hye; Park, Ae Kyung; Chi, Young Min; Moon, Jin Ho; Lee, Ki Seog.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 2, 01.02.2011, p. 214-216.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Psuedomonas aeruginosa
AU - Lee, Jeong Hye
AU - Park, Ae Kyung
AU - Chi, Young Min
AU - Moon, Jin Ho
AU - Lee, Ki Seog
PY - 2011/2/1
Y1 - 2011/2/1
N2 - During fatty-acid biosynthesis, enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the reduction of trans-2-enoyl-ACP to fully saturated acyl-ACP via the ubiquitous fatty-acid synthase system. NADH-dependent enoyl-ACP reductase (FabI) from Pseudomonas aeruginosa has been purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. Triclosan is an inhibitor of FabI and forms a stable ternary complex in the presence of NADH. The crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 Å, respectively. The crystals both belonged to space group P21, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 Å, Β = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 Å, Β = 116.162° for the complex. Preliminary molecular replacement further confirmed the presence of four tetramers of native FabI and one tetramer of the complex in the asymmetric unit, corresponding to Matthews coefficients (V M) of 2.46 and 2.05 Å 3 Da -1 and solvent contents of 50.1 and 40.1%, respectively.
AB - During fatty-acid biosynthesis, enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the reduction of trans-2-enoyl-ACP to fully saturated acyl-ACP via the ubiquitous fatty-acid synthase system. NADH-dependent enoyl-ACP reductase (FabI) from Pseudomonas aeruginosa has been purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. Triclosan is an inhibitor of FabI and forms a stable ternary complex in the presence of NADH. The crystals of native and complexed FabI diffracted to resolutions of 2.6 and 1.8 Å, respectively. The crystals both belonged to space group P21, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 Å, Β = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 Å, Β = 116.162° for the complex. Preliminary molecular replacement further confirmed the presence of four tetramers of native FabI and one tetramer of the complex in the asymmetric unit, corresponding to Matthews coefficients (V M) of 2.46 and 2.05 Å 3 Da -1 and solvent contents of 50.1 and 40.1%, respectively.
KW - Enoyl-acyl carrier protein reductases
KW - FabI
KW - Fatty-acid synthesis
KW - Pseudomonas aeruginosa
KW - Triclosan
UR - http://www.scopus.com/inward/record.url?scp=79951471300&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79951471300&partnerID=8YFLogxK
U2 - 10.1107/S1744309110048827
DO - 10.1107/S1744309110048827
M3 - Article
C2 - 21301088
AN - SCOPUS:79951471300
VL - 67
SP - 214
EP - 216
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 2
ER -