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

109 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

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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10.1093/emboj/17.4.977

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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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