1aux: Difference between revisions

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[[Image:1aux.gif|left|200px]]
{{Seed}}
[[Image:1aux.png|left|200px]]


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{{STRUCTURE_1aux|  PDB=1aux  |  SCENE=  }}  
{{STRUCTURE_1aux|  PDB=1aux  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9463376}}, adds the Publication Abstract to the page
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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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