1auv

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|PDB= 1auv |SIZE=350|CAPTION= <scene name='initialview01'>1auv</scene>, resolution 2.15&Aring;
|PDB= 1auv |SIZE=350|CAPTION= <scene name='initialview01'>1auv</scene>, resolution 2.15&Aring;
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auv OCA], [http://www.ebi.ac.uk/pdbsum/1auv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1auv RCSB]</span>
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[[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 Thu Mar 20 10:02:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:03 2008''

Revision as of 15:48, 30 March 2008


PDB ID 1auv

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN


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

1AUV 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

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