 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](tb5074fig4mag.jpg)
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Figure 4
(a) Structure-based sequence alignment of LmTBCA and the published structures of AtTBCA, ScRbl2p and HsTBCA. Residues highlighted in coloured boxes (blue, yellow and purple) are implicated in binding β-tubulin. Amino acids in orange boxes are thought to affect β-tubulin binding but are also located at the ScRbl2p homodimer interface. Cys58 is shown in red text and the location of the conserved proline (Pro80) is marked with a red triangle. Sequences were aligned with MUSCLE (Edgar, 2004  ) and the figure was prepared using ALINE (Bond & Schüttelkopf, 2009). (b) Stereo-image of LmTBCA helices α1 and α2 (red ribbon) with Cα backbone traces of AtTBCA (blue), ScRbl2p (yellow) and HsTBCA (purple). Selected residues are shown as sticks of the same colours labelled according to LmTBCA sequence and numbering. Residues at the corresponding positions of Asp39, Ala43 and Glu74 in LmTBCA appear to be critical for β-tubulin binding in A. thaliana. His81 and Ser82 are also thought to play a functional role (see text). Structural alignments were calculated using secondary-structure matching (Krissinel & Henrick, 2004). |
![[Figure 4]](tb5074fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
