 | Figure 3
Nature Structural Biology
9, 95 - 100 (2002)
Published online: 2 January 2001; | doi:10.1038/nsb744
Crystal structure of pea Toc34, a novel GTPase of the chloroplast protein transloconYuh-Ju Sun, Farhad Forouhar, Hsou-min Li, Shuh-Long Tu, Yi-Hong Yeh, Sen Kao, Hui-Lin Shr, Chia-Cheng Chou, Chinpan Chen
& Chwan-Deng Hsiao | | | | Figure 3. Sequence alignment of the Toc34/Toc159-G subfamily.
The secondary structural elements, deduced from this work (green), and those of Ras−GppNHp (PDB 5P21) (magenta) are shown above the sequences. Red and black asterisks represent residues from one monomer and the other monomer, respectively, interacting with GDP. Blue wavy lines above the sequences depict the G1−G5 motifs. Residues involved in Toc34 dimerization, shown below the sequences, are depicted as follows: red triangles for hydrogen bonding, blue stars for hydrophobic interaction and solid orange circles for van der Waals forces. The putative switches I and II are enclosed by light blue boxes, and the inserts I1−I6 are shown with a gray background. The longest loop (residues 209−230) between  6 and  6 is depicted as an orange line above the sequences, and the location of NKxD motif of Toc34 is shown by a red line below the sequences. All alignments were obtained using Pileup and Prettybox in GCG. The partial rice Toc34 sequence was obtained from the Monsanto Rice Genome Database.
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