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 4
Crystal packing of the ClpC1-NTD–RUF-I and ClpC1-NTD–ECU complexes. (a) The C^α trace of the protein in ClpC1-NTD–RUF-I depicts a close association of subunits. (b) The ClpC1-NTD–ECU complex has much more loosly associated subunits with no stable quaternary structure predicted. Both structures are a dimer of trimers or 32 symmetry. While the RUF-I complex has a staggered orientation (c), the ECU complex is eclipsed (d).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798320004027

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