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| | <StructureSection load='1pk8' size='340' side='right'caption='[[1pk8]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1pk8' size='340' side='right'caption='[[1pk8]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pk8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PK8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pk8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PK8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aux|1aux]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk8 OCA], [https://pdbe.org/1pk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1pk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pk8 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk8 OCA], [http://pdbe.org/1pk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1pk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pk8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYN1_RAT SYN1_RAT]] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. | + | [https://www.uniprot.org/uniprot/SYN1_RAT SYN1_RAT] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brautigam, C A]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Chelliah, Y]] | + | [[Category: Brautigam CA]] |
| - | [[Category: Deisenhofer, J]] | + | [[Category: Chelliah Y]] |
| - | [[Category: Atp binding]] | + | [[Category: Deisenhofer J]] |
| - | [[Category: Atp grasp]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
SYN1_RAT Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Synapsins are multidomain proteins that are critical for regulating neurotransmitter release in vertebrates. In the present study, two crystal structures of the C domain of rat synapsin I (rSynI-C) in complex with Ca(2+) and ATP reveal that this protein can form a tetramer and that a flexible loop (the "multifunctional loop") contacts bound ATP. Further experiments were carried out on a protein comprising the A, B, and C domains of rat synapsin I (rSynI-ABC). An ATP-stabilized tetramer of rSynI-ABC is observed during velocity sedimentation and size-exclusion chromatographic experiments. These hydrodynamic results also indicate that the A and B domains exist in an extended conformation. Calorimetric measurements of ATP binding to wild-type and mutant rSynI-ABC demonstrate that the multifunctional loop and a cross-tetramer contact are important for ATP binding. The evidence supports a view of synapsin I as an ATP-utilizing, tetrameric protein made up of monomers that have a flexible, extended N terminus.
Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I.,Brautigam CA, Chelliah Y, Deisenhofer J J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brautigam CA, Chelliah Y, Deisenhofer J. Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I. J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264 doi:10.1074/jbc.M312015200
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