Synapsin I is structurally similar to ATP-utilizing enzymes

Lothar Esser; Chyung Ru Wang; Masahiro Hosaka; Cynthia S. Smagula; Thomas C.südhof; Johann Deisenhofer

doi:10.1093/emboj/17.4.977

Synapsin I is structurally similar to ATP-utilizing enzymes

Lothar Esser, Chyung Ru Wang, Masahiro Hosaka, Cynthia S. Smagula, Thomas C.südhof, Johann Deisenhofer

Research output: Contribution to journal › Article › peer-review

111 Scopus citations

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 ATPγS and Ca²⁺ explains the preference of synC for Ca²⁺ over Mg²⁺. Our results suggest that synapsins may also be ATP-utilizing enzymes.

Original language	English (US)
Pages (from-to)	977-984
Number of pages	8
Journal	EMBO Journal
Volume	17
Issue number	4
DOIs	https://doi.org/10.1093/emboj/17.4.977
State	Published - Feb 4 1998

Keywords

ATP binding
Ca binding
Crystal structure
Structural similarity
Synaptic vesicle proteins

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
General Biochemistry, Genetics and Molecular Biology
General Immunology and Microbiology

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title = "Synapsin I is structurally similar to ATP-utilizing enzymes",

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 ATPγS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.",

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AU - Wang, Chyung Ru

AU - Hosaka, Masahiro

AU - Smagula, Cynthia S.

AU - C.südhof, Thomas

AU - Deisenhofer, Johann

PY - 1998/2/4

Y1 - 1998/2/4

N2 - 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 ATPγS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.

AB - 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 ATPγS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.

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KW - Ca binding

KW - Crystal structure

KW - Structural similarity

KW - Synaptic vesicle proteins

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Synapsin I is structurally similar to ATP-utilizing enzymes

Abstract

Keywords

ASJC Scopus subject areas

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