Intracellular proteolysis carried out by energy-dependent proteases is one of the most
conserved biological processes. In all cells proteolysis maintains and shapes the cellular …

Covering: up to 2017 The bacterial Clp protease is a highly conserved and structurally
versatile machine. It has gained a lot of recognition during the last decade as a novel …

The treatment of postoperative infection caused by multidrug‐resistant bacteria, such as
methicillin‐resistant Staphylococcus aureus (MRSA), has become an intractable clinical …

The emergence of methicillin-resistant Staphylococcus aureus isolates highlights the urgent
need to develop more antibiotics. ClpP is a highly conserved protease regulated by …

The Clp protease complex degrades a multitude of substrates, which are engaged by a
AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped …

Acyldepsipeptides (ADEPs) are potential antibiotics that dysregulate the activity of the highly
conserved tetradecameric bacterial ClpP protease, leading to bacterial cell death. Here, we …

The ClpXP machinery is a two-component protease complex that performs targeted protein
degradation in bacteria and mitochondria. The complex consists of the AAA+ chaperone …

Rice bacterial leaf blight caused by Xanthomonas oryzae pv. oryzae (Xoo) is considered a
destructive plant bacterial disease. The looming crisis of antibiotic resistance necessitates …

Coordinated conformational transitions in oligomeric enzymatic complexes modulate
function in response to substrates and play a crucial role in enzyme inhibition and activation …

ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-
dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self …