1cjw

SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOGSEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG

Structural highlights 1cjw is a 1 chain structure with sequence from Ovis aries. The January 2008 RCSB PDB Molecule of the Month feature on Circadian Clock Proteins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SNAT_SHEEP Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone. Comparison of the structures of the substrate-free enzyme and the complex with a bisubstrate analog, coenzyme A-S-acetyltryptamine, demonstrates that acetyl coenzyme A (AcCoA) binding is accompanied by a large conformational change that in turn leads to the formation of the serotonin-binding site. The structure of the complex also provides insight into how the enzyme may facilitate acetyl transfer. A water-filled channel leading from the active site to the surface provides a pathway for proton removal following amine deprotonation. Furthermore, structural and mutagenesis results indicate an important role for Tyr-168 in catalysis. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.,Hickman AB, Namboodiri MA, Klein DC, Dyda F Cell. 1999 Apr 30;97(3):361-9. PMID:10319816 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serotonin N-acetyltransferase

spinqualitylabelsall models 1cjw, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image