Structural and Functional Characterization of an Ancient Bacterial Transglutaminase Sheds Light on the Minimal Requirements for Protein Cross-Linking

Transglutaminases are best known for their ability to catalyze protein cross-linking reactions that impart chemical and physical resilience to cellular structures. Here, we report the crystal structure and characterization of Tgl, a transglutaminase from the bacterium Bacillus subtilis. Tgl is produ...

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Veröffentlicht in:	Biochemistry (Easton) 2015-09, Vol.54 (37), p.5723-5734
Hauptverfasser:	Fernandes, Catarina G, Plácido, Diana, Lousa, Diana, Brito, José A, Isidro, Anabela, Soares, Cláudio M, Pohl, Jan, Carrondo, Maria A, Archer, Margarida, Henriques, Adriano O
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus Bacillus subtilis Bacillus subtilis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Catalytic Domain Cross-Linking Reagents - chemistry Crystallography, X-Ray Hydrophobic and Hydrophilic Interactions Molecular Dynamics Simulation Point Mutation Protein Conformation Protein Folding Transglutaminases - chemistry Transglutaminases - genetics
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