Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions

Wolf, N.M.; Lee, H.; Zagal, D.; Nam, J.-W.; Oh, D.-C.; Lee, H.; Suh, J.-W.; Pauli, G.F.; Cho, S.; Abad-Zapatero, C.

doi:10.1107/S2059798320004027

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
SPR binding of ClpC1 mutants to macrocyclic peptides. (a) ClpC1-FL with various sites mutated was immobilized, while the cyclopeptide (ECU in blue, RUF-I in lilac and OMS-A in yellow) was passed over the surface. Averages of three titrations are shown with standard deviations in black. (b) ClpC1-NTD with mutations at the N-terminus was also titrated with the cyclopeptides. Wild-type (WT) results are plotted for reference.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 76| Part 5| May 2020| Pages 458-471

https://doi.org/10.1107/S2059798320004027

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