Structural highlights
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
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.
Synapsin I is structurally similar to ATP-utilizing enzymes.,Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J EMBO J. 1998 Feb 16;17(4):977-84. PMID:9463376[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J. Synapsin I is structurally similar to ATP-utilizing enzymes. EMBO J. 1998 Feb 16;17(4):977-84. PMID:9463376 doi:10.1093/emboj/17.4.977
