The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.

Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H
J Biol Chem 293(22):8379-8393 (2018 Jun 1)
PMID: 29632076
doi: 10.1074/jbc.RA118.002251
Submitted to SASBDB: 2018 Jan 24
Published in SASBDB:

SASDD93 – ATP-dependent Clp protease ATP-binding subunit ClpC1

ATP-dependent Clp protease ATP-binding subunit ClpC1 experimental SAS data
OTHER model
Sample: ATP-dependent Clp protease ATP-binding subunit ClpC1, 95 kDa Mycobacterium tuberculosis protein
Buffer: Hepes 50 mM pH 7.5, KCl 100 mM, glycerol 10%, MgCl2 4 mM and ATP 1 mM, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Sep 18
RgGuinier 7.6 nm
Dmax 25.0 nm
VolumePorod 2156 nm3

SASDDA3 – ATP-dependent Clp protease ATP-binding subunit ClpC1, second state

ATP-dependent Clp protease ATP-binding subunit ClpC1 experimental SAS data
ATP-dependent Clp protease ATP-binding subunit ClpC1 Kratky plot
Sample: ATP-dependent Clp protease ATP-binding subunit ClpC1, 95 kDa Mycobacterium tuberculosis protein
Buffer: Hepes 50 mM pH 7.5, KCl 100 mM, glycerol 10%, MgCl2 4 mM and ATP 1 mM, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Sep 18
RgGuinier 7.9 nm
Dmax 25.1 nm
VolumePorod 2416 nm3