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1.
Proc Natl Acad Sci U S A ; 101(1): 59-64, 2004 Jan 06.
Article in English | MEDLINE | ID: mdl-14684831

ABSTRACT

The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, homologous to eukaryotic subunit d of V-ATPases, has been determined at 1.95-A resolution and located into the holoenzyme complex structure obtained by single particle analysis as suggested by the results of subunit cross-linking experiments. The result shows that V-ATPase is substantially longer than the related F-type ATPase, due to the insertion of subunit C between the V(1) (soluble) and the V(o) (membrane bound) domains. Subunit C, attached to the V(o) domain, seems to have a socket like function in attaching the central-stalk subunits of the V(1) domain. This architecture seems essential for the reversible association/dissociation of the V(1) and the V(o) domains, unique for V-ATPase activity regulation.


Subject(s)
Vacuolar Proton-Translocating ATPases/chemistry , Base Sequence , Cross-Linking Reagents , Crystallography, X-Ray , DNA, Bacterial/genetics , Holoenzymes/chemistry , Holoenzymes/genetics , Holoenzymes/metabolism , Microscopy, Electron , Models, Molecular , Mutagenesis, Site-Directed , Protein Subunits , Static Electricity , Thermus thermophilus/enzymology , Thermus thermophilus/genetics , Vacuolar Proton-Translocating ATPases/genetics , Vacuolar Proton-Translocating ATPases/metabolism
2.
Acta Crystallogr D Biol Crystallogr ; 59(Pt 3): 600-2, 2003 Mar.
Article in English | MEDLINE | ID: mdl-12595738

ABSTRACT

The membrane-bound respiratory complex II, succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 A, and diffract to 2.6 A resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.


Subject(s)
Escherichia coli/enzymology , Multienzyme Complexes/chemistry , Oxidoreductases/chemistry , Succinate Dehydrogenase/chemistry , Anisotropy , Coloring Agents , Crystallization , Crystallography, X-Ray , Electron Transport Complex II , Microscopy, Electron , Multienzyme Complexes/isolation & purification , Oxidoreductases/isolation & purification , Succinate Dehydrogenase/isolation & purification , Ultracentrifugation
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