1AUX

STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND

Summary for 1AUX

• Entry DOI: 10.2210/pdb1aux/pdb
• Descriptor: SYNAPSIN IA, CALCIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: synapse, phosphorylation, synapsin ia c-domain, atp-binding, transferase
• Biological source: Bos taurus (cattle)
• Cellular location: Cell junction, synapse: P17599
• Total number of polymer chains: 2
• Total formula weight: 70930.61

Authors

Esser, L.,Wang, C.,Deisenhofer, J. (deposition date: 1997-09-06, release date: 1998-03-18, Last modification date: 2024-05-22)

Primary citation

Esser, L.,Wang, C.R.,Hosaka, M.,Smagula, C.S.,Sudhof, T.C.,Deisenhofer, J.
Synapsin I is structurally similar to ATP-utilizing enzymes.
EMBO J., 17:977-984, 1998

PubMed 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.

PubMed: 9463376
DOI: 10.1093/emboj/17.4.977

Experimental method

X-RAY DIFFRACTION (2.3 Å)