3u3o

Crystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7-hydroxycoumarinCrystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7-hydroxycoumarin

Structural highlights 3u3o is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 3u3j, 3u3k, 3u3m, 3u3r Gene: hSULT1A1, OK/SW-cl.88, STP, STP1, SULT1A1 (HUMAN) Activity: Aryl sulfotransferase, with EC number 2.8.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ST1A1_HUMAN] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk. Publication Abstract from PubMed Cytosolic sulfotransferases (SULTs) are mammalian enzymes that detoxify a wide variety of chemicals through the addition of a sulfate group. Despite extensive research, the molecular basis for the broad specificity of SULTs is still not understood. Here, structural, protein engineering and kinetic approaches were employed to obtain deep understanding of the molecular basis for the broad specificity, catalytic activity and substrate inhibition of SULT1A1. We have determined five new structures of SULT1A1 in complex with different acceptors, and utilized a directed evolution approach to generate SULT1A1 mutants with enhanced thermostability and increased catalytic activity. We found that active site plasticity enables binding of different acceptors and identified dramatic structural changes in the SULT1A1 active site leading to the binding of a second acceptor molecule in a conserved yet non-productive manner. Our combined approach highlights the dominant role of SULT1A1 structural flexibility in controlling the specificity and activity of this enzyme. The molecular basis for the broad substrate specificity of human sulfotransferase 1A1.,Berger I, Guttman C, Amar D, Zarivach R, Aharoni A PLoS One. 2011;6(11):e26794. Epub 2011 Nov 1. PMID:22069470 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfotransferase 3D structures

spinqualitylabelsall models 3u3o, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image