The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog

Article Abstract:

A study was conducted to examine the structure of the serotonin N-acetyltransferase (arylalkylamine-N-acetyltransferase[AANAT]). Results show that there is a bisubstrate analog bound to AANAT's enzyme active site, which was synthesized covalently binding the N-acetylated substrate, tryptamine and coenzyme A. It was also observed that analysis of the structure of the complex with bisubstrate analog will be useful in understanding the nature of substrate binding and the mechanism of enzyme action.

Coenzymes

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Crystal structure of the 14-3-3(zeta):serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation

Article Abstract:

Research has been conducted on the serotonin N-acetyltransferase which controls the melatonin synthesis rhythm. The structure of the serotonin N-acetyltransferase bound to the phosphorylation dependent association 14-3-3(zeta) has been determined and the results of the crystallographic analysis indicate that this binding modulates serotonin N-acetyltransferase's activity and affinity for its substrates.

Statistical Data Included, Analysis, Physiological aspects, Enzymes, Cell research, Cytological research, Nitrogen, Scaffolding

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Structural and functional organization of the ESCRT-I trafficking complex

Article Abstract:

The structural and functional results presented provide a picture of the organization of the ESCRT-1 complex, which is the central to receptor downregulation, lysosome biogenesis, and budding of HIV. It is found that the fundamental unit of the ESCRT-1 complex is a 1:1:1 heterotrimer, which appears to be capable of forming weakly interacting dimers in vitro and higher order oligomers in vivo.

Science & research, Life, Lysosomes, Origin of life, Oligomers

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