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Figure 3
Structural comparison of the AtTae4–AtTai4 complex with the SmTae4–SmTai4 complex. (a) A superimposition of AtTai4 and SmTai4 indicated that AtTai4 contains extensions in the α2 helix and in the loop between the α1 and α2 helices. (b) The residues involved in the interaction between AtTai4 and AtTae4. (c) The crystal structure of the SmTae4–SmTai4 complex revealed that Gln84 of SmTai4 interacts with His133 of SmTae4 and blocks the active site (PDB entry 4bi8; Srikannathasan et al., 2013BB16). (d) The crystal structure of the AtTae4–AtTai4 complex lacks the interaction between the expected catalytic His131 of AtTae4 and the corresponding residue of AtTai4. The glutamine is not conserved in AtTai4 and is replaced by an alanine in AtTai4. (e) The AtTai4 homodimer is positioned close to the AtTae4 active-site surface and may block substrate binding.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 74| Part 12| December 2018| Pages 810-816
https://doi.org/10.1107/S2053230X18016369
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