Results: 4

1.
FIGURE 3.

FIGURE 3. From: Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides.

Electron density maps calculated with regions of the model omitted. Stereo images showing the electron density omit maps calculated excluding residues βVal-371–Leu-391 (A) and βSer-340–Pro-350, and βGlu-422–Pro-428 (B) along with the pertinent regions of the final model are shown. The 2Fo - Fc maps are contoured at 1 σ.

Venkataraman Kabaleeswaran, et al. J Biol Chem. 2009 April 17;284(16):10546-10551.
2.
FIGURE 4.

FIGURE 4. From: Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides.

Conformational changes of the γ subunit. A, a comparison of the structure of the γ subunit from the ground state structure (yellow) with that from nucleotide-free F1 ATPase (green). B, a comparison of the γ subunit from the nucleotide-free structure from Complex I (green) and Complex II (red). In both cases, the structures were superposed using the β-barrel domains of the α and β subunits. Helices and selected residues are labeled.

Venkataraman Kabaleeswaran, et al. J Biol Chem. 2009 April 17;284(16):10546-10551.
3.
FIGURE 2.

FIGURE 2. From: Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides.

Comparison of the structures of ground state and nucleotide-free yeast F1 ATPase. Pairs of α/β subunits are shown after superposition of the N-terminal β-barrel domains. The ground state structure is shown in yellow, and the structures of the α and β subunits of the nucleotide-free enzyme are shown in red and blue, respectively. Panels A, C, and E show the α-carbon traces for the αDPDP, αTPTP, and αEE subunit pairs, respectively. In panels A and C, shaded regions show the location of the nucleotide-binding sites. Panels B and D show the region around the active site with the side chains shown only for the ground state structure. The arrow indicates the shift of the Cα backbone at residue βPhe-424.

Venkataraman Kabaleeswaran, et al. J Biol Chem. 2009 April 17;284(16):10546-10551.
4.
FIGURE 1.

FIGURE 1. From: Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides.

Electron density at the catalytic sites of yeast F1 ATPase in the absence of nucleotides. In each panel, the 2Fo - Fc map is shown (contoured at 1 σ) with the position of the nucleotide modeled from the ground state structure. The inset plots show the region where the nucleotide would bind and corresponding electron density. The main chain is represented as a ribbon in red and blue for the α and β subunits, respectively. The side chains of selected residues important for substrate binding and catalysis are shown. A, αDPDP site; B, αTPTP site; C, a noncatalytic (NC) site, all for Complex I. D, the phosphate-binding site in the αEE site of Complex II.

Venkataraman Kabaleeswaran, et al. J Biol Chem. 2009 April 17;284(16):10546-10551.

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