| Literature DB >> 9463376 |
L Esser1, C R Wang, M Hosaka, C S Smagula, T C Südhof, J Deisenhofer.
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 ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.Entities:
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Year: 1998 PMID: 9463376 PMCID: PMC1170447 DOI: 10.1093/emboj/17.4.977
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598