PMID:11803025
| Citation |
Törnroth, S, Yankovskaya, V, Cecchini, G and Iwata, S (2002) Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli. Biochim. Biophys. Acta 1553:171-6 |
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| Abstract |
A membrane protein complex, succinate dehydrogenase (SQR) from Escherichia coli has been purified and crystallised. This enzyme is composed of four subunits containing FAD, three iron-sulphur clusters and one haem b as prosthetic groups. The obtained crystals belong to the hexagonal space group P6(3) with the unit-cell dimensions of a=b=123.8 A and c=214.6 A. An asymmetric unit of the crystals contains one SQR monomer (M(r) 120 kDa). A data set is now available at 4.0 A resolution with 88.1% completeness and 0.106 R(merge). We have obtained a molecular replacement solution that shows sensible molecular packing, using the soluble domain of E. coli QFR (fumarate reductase) as a search model. The packing suggests that E. coli SQR is a crystallographic trimer rather than a dimer as observed for the E. coli QFR. |
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| Keywords |
Crystallography; Electron Transport Complex II; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/chemistry; Fumarates/chemistry; Fumarates/metabolism; Heme/chemistry; Intracellular Membranes/enzymology; Iron-Sulfur Proteins/chemistry; Membrane Proteins/chemistry; Models, Molecular; Multienzyme Complexes/chemistry; Multienzyme Complexes/isolation & purification; Oxidoreductases/chemistry; Oxidoreductases/isolation & purification; Quinone Reductases/chemistry; Quinone Reductases/isolation & purification; Succinate Dehydrogenase/chemistry; Succinate Dehydrogenase/isolation & purification; Succinic Acid/chemistry; Succinic Acid/metabolism |
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