Intricate Structure–Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria

• Published in: International journal of molecular sciences Vol. 25; no. 23; p. 13182
• Main Authors: Zarzecka, Urszula, Skorko-Glonek, Joanna
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.12.2024
• Subjects: Aspartic proteinases; Bacteria; Bacterial infections; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; E coli; Enzymes; Escherichia coli; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Gram-negative bacteria; Gram-Negative Bacteria - metabolism; Health aspects; Humans; Models, Molecular; Peptides; Protein Conformation; Proteins; Proteolysis; RNA polymerase; Serine Endopeptidases - chemistry; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Signal transduction; Structure-Activity Relationship; Virulence; Virulence (Microbiology); regulation of activity; oligomerization; HtrA; Gram-negative bacteria; PDZ domain; serine protease; regulatory loops; allostery
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms252313182

Proteolytic enzymes play key roles in living organisms. Because of their potentially destructive action of degrading other proteins, their activity must be very tightly controlled. The evolutionarily conserved proteins of the HtrA family are an excellent example illustrating strategies for regulatin...