1auv
|
STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN
OverviewOverview
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.
About this StructureAbout this Structure
1AUV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Tue Nov 20 11:08:45 2007