Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins.

doi:10.1016/j.jsb.2017.11.003

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Article

Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins.

Journal of structural biology - 1 Jan 2018

Miller Justin M, Chaudhary Hamza, Marsee Justin D

Abstract excerpt

Regulated proteolysis is required in all organisms for the removal of misfolded or degradation-tagged protein substrates in cellular quality control pathways. The molecular machines that catalyze this process are known as ATP-dependent proteases with examples that include ClpAP and ClpCP. Clp/Hsp100 subunits form ring-structures that couple the energy of ATP binding and hydrolysis to protein unfolding and...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Amino Acid Sequence
Bacterial Proteins
Endopeptidase Clp
Genetic Variation
Heat-Shock Proteins
Hydrolysis
Phylogeny
Protein Binding
Protein Domains
Protein Unfolding
Proteobacteria
Sequence Homology, Amino Acid
Species Specificity

Source

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Identifiers

PMID: 29129755
DOI: 10.1016/j.jsb.2017.11.003

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