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1aux

From Proteopedia

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[[Image:1aux.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1aux| PDB=1aux | SCENE= }}
{{STRUCTURE_1aux| PDB=1aux | SCENE= }}
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'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND'''
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===STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9463376}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9463376 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9463376}}
==About this Structure==
==About this Structure==
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[[Category: Synapse]]
[[Category: Synapse]]
[[Category: Synapsin ia c-domain]]
[[Category: Synapsin ia c-domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:43:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:38:30 2008''

Revision as of 14:38, 30 June 2008

Image:1aux.png

Template:STRUCTURE 1aux

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

Template:ABSTRACT PUBMED 9463376

About this Structure

1AUX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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 Mon Jun 30 17:38:30 2008

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