Sandbox Reserved 494: Difference between revisions
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The first atomic-level(2.8Å) resolution structures by '''<FONT COLOR="#F87217">X-ray</FONT>''', strucutures was of bovine mitochondrial F<sub>1</sub> in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''<FONT COLOR="#571B7e">NMR</FONT>''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by SDS-polyacrylamide gel electrophoresis '''<FONT COLOR="#E42217"> (SDS-PAGE) </FONT>''', high-performance liquid chromatography'''<FONT COLOR="#F535AA">(HPLC)</FONT>''' analysis, and NH<sub>2</sub>-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c(in diminishing apparent molecular weight order for F<sub>1</sub> and F<sub>0</sub> on SDS gels) and is similar to other preparations. | The first atomic-level(2.8Å) resolution structures by '''<FONT COLOR="#F87217">X-ray</FONT>''', strucutures was of bovine mitochondrial F<sub>1</sub> in 1994. The α and β subunits each had similiar three-domain structure, with an N-terminal β-barrel furthest away from the membrane surface, a central nucleotide-binding domain, and a C-terminal helical domain. Also, an '''<FONT COLOR="#571B7e">NMR</FONT>''' structure of isolated ''E. coli'' ε subunit is in good agreement with X-ray structure. The structure of the N-terminal domain of ''E. coli'' δ subunit consisting of residues 1 through 134 was solved also by NMR <ref name="MM"/>. In addition, according to analyses by SDS-polyacrylamide gel electrophoresis '''<FONT COLOR="#E42217"> (SDS-PAGE) </FONT>''', high-performance liquid chromatography'''<FONT COLOR="#F535AA">(HPLC)</FONT>''' analysis, and NH<sub>2</sub>-terminal sequencing, the purified complex used here for crystallization consists of subunis α, β, γ, δ, ε, b, d, a, h, f, ATP8, and c(in diminishing apparent molecular weight order for F<sub>1</sub> and F<sub>0</sub> on SDS gels) and is similar to other preparations. | ||
== | ==Reaction analysis of the catalytic sites== | ||
When the magnitude of △H is large, as in functionalmitochondrial, downhill proton flow through F<sub>0</sub> causes rotation of the F<sub>0</sub> rotor and hence rotation of the γε-subunits of F<sub>1</sub>. The rotary motion of the γ alternates the structure of the β-subunit so the ATP is synthesized<ref>PMID: 12788493</ref>. | When the magnitude of △H is large, as in functionalmitochondrial, downhill proton flow through F<sub>0</sub> causes rotation of the F<sub>0</sub> rotor and hence rotation of the γε-subunits of F<sub>1</sub>. The rotary motion of the γ alternates the structure of the β-subunit so the ATP is synthesized<ref>PMID: 12788493</ref>. | ||
