4OBU

Ruminococcus gnavus tryptophan decarboxylase RUMGNA_01526 (apo)

Summary for 4OBU

• Entry DOI: 10.2210/pdb4obu/pdb
• Related: 4OBV
• Descriptor: Pyridoxal-dependent decarboxylase domain protein, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: type 1 plp-dependent, decarboxylase, tryptophan, lyase
• Biological source: Ruminococcus gnavus
• Total number of polymer chains: 8
• Total formula weight: 442174.10

Authors

Van Benschoten, A.H.,Fraser, J.S. (deposition date: 2014-01-07, release date: 2014-10-29, Last modification date: 2024-02-28)

Primary citation

Williams, B.B.,Van Benschoten, A.H.,Cimermancic, P.,Donia, M.S.,Zimmermann, M.,Taketani, M.,Ishihara, A.,Kashyap, P.C.,Fraser, J.S.,Fischbach, M.A.
Discovery and Characterization of Gut Microbiota Decarboxylases that Can Produce the Neurotransmitter Tryptamine.
Cell Host Microbe, 16:495-503, 2014

PubMed Abstract: Several recent studies describe the influence of the gut microbiota on host brain and behavior. However, the mechanisms responsible for microbiota-nervous system interactions are largely unknown. Using a combination of genetics, biochemistry, and crystallography, we identify and characterize two phylogenetically distinct enzymes found in the human microbiome that decarboxylate tryptophan to form the β-arylamine neurotransmitter tryptamine. Although this enzymatic activity is exceedingly rare among bacteria more broadly, analysis of the Human Microbiome Project data demonstrate that at least 10% of the human population harbors at least one bacterium encoding a tryptophan decarboxylase in their gut community. Our results uncover a previously unrecognized enzymatic activity that can give rise to host-modulatory compounds and suggests a potential direct mechanism by which gut microbiota can influence host physiology, including behavior.

PubMed: 25263219
DOI: 10.1016/j.chom.2014.09.001

Experimental method

X-RAY DIFFRACTION (2.804 Å)