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1aux

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(New page: 200px<br /><applet load="1aux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aux, resolution 2.30&Aring;" /> '''STRUCTURE OF THE C D...)
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Revision as of 09:01, 20 November 2007

Image:1aux.gif

1aux, resolution 2.30Å

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

Overview

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.

About this Structure

1AUX is a Single protein structure of sequence from Bos taurus with CA and SAP as ligands. 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

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