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1aux
From Proteopedia
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| - | [[Image:1aux.gif|left|200px]] | + | [[Image:1aux.gif|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND''' | + | {{Structure |
| + | |PDB= 1aux |SIZE=350|CAPTION= <scene name='initialview01'>1aux</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE'>SAP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AUX is a [ | + | 1AUX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9463376 9463376] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: synapsin ia c-domain]] | [[Category: synapsin ia c-domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:34 2008'' |
Revision as of 08:02, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 10:02:34 2008
Categories: Bos taurus | Single protein | Deisenhofer, J. | Esser, L. | Wang, C. | CA | SAP | Atp-binding | Calcium | Phosphorylation | Synapse | Synapsin ia c-domain
