PDBsum entry: 1auv

Synapse

PDB id: 1auv

Contents

Protein chains

292 a.a. *

Waters ×161

* Residue conservation analysis

PDB id:

1auv

Name:

Synapse

Title:

Structure of thE C domain of synapsin ia from bovine brain

Structure:

Synapsin ia. Chain: a, b. Fragment: residues 110 - 420. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Cell_line: b834. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.15Å R-factor: 0.199 R-free: 0.255

Authors:

L.Esser,C.Wang,J.Deisenhofer

Key ref:

L.Esser et al. (1998). Synapsin I is structurally similar to ATP-utilizing enzymes. EMBO J, 17, 977-984. PubMed id: 9463376 DOI: 10.1093/emboj/17.4.977

Date:

02-Sep-97 Release date: 18-Mar-98

Protein chains

P17599  (SYN1_BOVIN) -  Synapsin-1

Seq: 706 a.a.

Struc: 292 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Cellular component: synaptic vesicle (1 term)
• Biological process: neurotransmitter secretion (1 term)
• Biochemical function: catalytic activity (3 terms)

DOI no: 10.1093/emboj/17.4.977

EMBO J 17:977-984 (1998)

PubMed id: 9463376

Synapsin I is structurally similar to ATP-utilizing enzymes.

L.Esser, 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.

Selected figure(s)

Figure 1.
Figure 1 Ribbon diagrams of the monomers of (A) synC and (B) the complex of glutathione synthetase with MgADP and glutathione as ball-and-stick models (PDB entry 1gsa). (C) Stereo drawing of the C -trace of synC, colored yellow to blue from the amino- to the carboxy-terminus; a ball-and stick model in atom colors of bound ATP S is also shown. Selected C -atoms are marked with red balls and residue numbers. (D) Topology diagram of synC. Disordered residues are indicated by dotted lines. (A), (B) and Figure 4 were made with a modified version of the program Molscript (Esnouf, 1997).

Figure 4.
Figure 4 Schematic drawing of a tight dimer of CaATP S viewed down the crystallographic 2-fold axis. Monomers are colored blue and brown, with the ligands drawn as ball-and-stick models.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1998, 17, 977-984) copyright 1998.

Figures were selected by an automated process.