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S100B, an EF-hand Ca2+-binding protein, grasps the C-terminus of the tumor suppressor p53 and inhibits protein kinase C-dependent phosphorylation and acetylation of p53 in a Ca2+-dependent manner. The mode of interaction between S100B and p53 is different from the interactions seen in S100A–annexin complex structures.
The crystal structure of TolC, one of the most mysterious proteins in the outer membrane of Gram-negative bacteria, suggests a mechanism for its role in secretion of proteins and efflux of toxic chemicals.
Some prokaryotic transcriptional activators act by binding to enhancers and directly changing the conformation of a specialized sigma factor in the RNA polymerase holoenzyme. This mechanism has interesting parallels in other transcription systems.
The first high resolution structure of an ATP-dependent cation pump of the P-type family — the Ca2+-ATPase from the sarcoplasmic reticulum of rabbit muscle — has now been determined.
