Synapsin I is structurally similar to ATP-utilizing enzymes

Lothar Esser, Chyung Ru Wang, Masahiro Hosaka, Cynthia S. Smagula, Thomas C.südhof, Johann Deisenhofer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

108 Scopus citations

Abstract

Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPγS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.

Original languageEnglish (US)
Pages (from-to)977-984
Number of pages8
JournalEMBO Journal
Volume17
Issue number4
DOIs
StatePublished - Feb 4 1998

Keywords

  • ATP binding
  • Ca binding
  • Crystal structure
  • Structural similarity
  • Synaptic vesicle proteins

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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