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Author (up) Kaczmarska, Z.; Ortega, E.; Goudarzi, A.; Huang, H.; Kim, S.; Márquez, J.A.; Zhao, Y.; Khochbin, S.; Panne, D. url  openurl
  Title Structure of p300 in complex with acyl-CoA variants Type Journal Article
  Year 2017 Publication Abbreviated Journal Nature Chemical Biology  
  Volume 13 Issue 27820805 Pages 21--29  
  Keywords pdb,structural biology,variant assessment  
  Abstract Histone acetylation plays an important role in transcriptional activation. Histones are also modified by chemically diverse acylations that are frequently deposited by p300, a transcriptional coactivator that uses a number of different acyl-CoA cofactors. Here we report that while p300 is a robust acetylase, its activity gets weaker with increasing acyl-CoA chain length. Crystal structures of p300 in complex with propionyl-, crotonyl-, or butyryl-CoA show that the aliphatic portions of these cofactors are bound in the lysine substrate-binding tunnel in a conformation that is incompatible with substrate transfer. Lysine substrate binding is predicted to remodel the acyl-CoA ligands into a conformation compatible with acyl-chain transfer. This remodeling requires that the aliphatic portion of acyl-CoA be accommodated in a hydrophobic pocket in the enzymes active site. The size of the pocket and its aliphatic nature exclude long-chain and charged acyl-CoA variants, presumably explaining the cofactor preference for p300.  
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  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 1552-4450 ISBN Medium  
  Area Expedition Conference  
  Notes Approved no  
  Call Number AG @ matthewjvarga @ Serial 47189  
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