2Y1Q

Crystal Structure of ClpC N-terminal Domain

Summary for 2Y1Q

• Entry DOI: 10.2210/pdb2y1q/pdb
• Related: 2Y1R
• Descriptor: NEGATIVE REGULATOR OF GENETIC COMPETENCE CLPC/MECB, SULFATE ION (3 entities in total)
• Functional Keywords: transcription, proteolysis
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 16838.11

Authors

Wang, F.,Mei, Z.Q.,Wang, J.W.,Shi, Y.G. (deposition date: 2010-12-10, release date: 2011-03-16, Last modification date: 2024-05-08)

Primary citation

Wang, F.,Mei, Z.,Qi, Y.,Yan, C.,Hu, Q.,Wang, J.,Shi, Y.
Structure and Mechanism of the Hexameric Meca-Clpc Molecular Machine.
Nature, 471:331-, 2011

PubMed Abstract: Regulated proteolysis by ATP-dependent proteases is universal in all living cells. Bacterial ClpC, a member of the Clp/Hsp100 family of AAA+ proteins (ATPases associated with diverse cellular activities) with two nucleotide-binding domains (D1 and D2), requires the adaptor protein MecA for activation and substrate targeting. The activated, hexameric MecA-ClpC molecular machine harnesses the energy of ATP binding and hydrolysis to unfold specific substrate proteins and translocate the unfolded polypeptide to the ClpP protease for degradation. Here we report three related crystal structures: a heterodimer between MecA and the amino domain of ClpC, a heterododecamer between MecA and D2-deleted ClpC, and a hexameric complex between MecA and full-length ClpC. In conjunction with biochemical analyses, these structures reveal the organizational principles behind the hexameric MecA-ClpC complex, explain the molecular mechanisms for MecA-mediated ClpC activation and provide mechanistic insights into the function of the MecA-ClpC molecular machine. These findings have implications for related Clp/Hsp100 molecular machines.

PubMed: 21368759
DOI: 10.1038/NATURE09780

Experimental method

X-RAY DIFFRACTION (1.5 Å)