1aux: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1aux |SIZE=350|CAPTION= <scene name='initialview01'>1aux</scene>, resolution 2.30Å | |PDB= 1aux |SIZE=350|CAPTION= <scene name='initialview01'>1aux</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE+MONOTHIOPHOSPHATE'>SAP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aux OCA], [http://www.ebi.ac.uk/pdbsum/1aux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aux RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Esser, L.]] | [[Category: Esser, L.]] | ||
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
| Line 33: | Line 34: | ||
[[Category: synapsin ia c-domain]] | [[Category: synapsin ia c-domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:58 2008'' | ||
Revision as of 18:48, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND
OverviewOverview
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 StructureAbout this Structure
1AUX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun Mar 30 18:47:58 2008