Unknown

Dataset Information

0

Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH.

ABSTRACT: FabG4 from Mycobacterium tuberculosis belongs to the high molecular weight ketoacyl reductases (HMwFabGs). The enzyme requires NADH for ?-ketoacyl reductase activity. The protein was overexpressed, purified to homogeneity and crystallized as a FabG4-NADH complex. A mountable FabG4:NADH complex crystal diffracted to 2.59?Å resolution and belonged to space group P1, with unit-cell parameters a = 63.07, b = 71.03, c = 92.92?Å, ? = 105.02, ? = 97.06, ? = 93.66°. The Matthews coefficient suggested the presence of four monomers in the unit cell. In addition, a self-rotation function revealed the presence of two twofold NCS axes and one fourfold NCS axis. At ? = 180° the highest peak corresponds to the twofold NCS between two monomers, whereas the second peak corresponds to the twofold NCS between two dimers.

SUBMITTER: Dutta D 

PROVIDER: S-EPMC3388922 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH.

Dutta Debajyoti D   Bhattacharyya Sudipta S   Das Amit Kumar AK  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120627 Pt 7

FabG4 from Mycobacterium tuberculosis belongs to the high molecular weight ketoacyl reductases (HMwFabGs). The enzyme requires NADH for β-ketoacyl reductase activity. The protein was overexpressed, purified to homogeneity and crystallized as a FabG4-NADH complex. A mountable FabG4:NADH complex crystal diffracted to 2.59 Å resolution and belonged to space group P1, with unit-cell parameters a = 63.07, b = 71.03, c = 92.92 Å, α = 105.02, β = 97.06, γ = 93.66°. The Matthews coefficient suggested th  ...[more]

Similar Datasets

Unknown Crystallization and preliminary X-ray diffraction analysis of Trap1 complexed with Hsp90 inhibitors.
| S-EPMC4259240 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase.
| S-EPMC2339750 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.
| S-EPMC2242957 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of Salmonella typhimurium uridine phosphorylase complexed with 5-fluorouracil.
| S-EPMC2688420 | biostudies-literature
Unknown Purification, crystallization and preliminary X-ray diffraction analysis of 3-ketoacyl-CoA thiolase A1887 from Ralstonia eutropha H16.
| S-EPMC4461343 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of (R)-carbonyl reductase from Candida parapsilosis.
| S-EPMC4051541 | biostudies-literature
Unknown Crystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5.
| S-EPMC2330128 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.
| S-EPMC2335014 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.
| S-EPMC2815683 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor.
| S-EPMC3001671 | biostudies-literature