1px2: Difference between revisions
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|PDB= 1px2 |SIZE=350|CAPTION= <scene name='initialview01'>1px2</scene>, resolution 2.23Å | |PDB= 1px2 |SIZE=350|CAPTION= <scene name='initialview01'>1px2</scene>, resolution 2.23Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SYN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= SYN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1pk8|1PK8]], [[1aux|1AUX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1px2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px2 OCA], [http://www.ebi.ac.uk/pdbsum/1px2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1px2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Chelliah, Y.]] | [[Category: Chelliah, Y.]] | ||
[[Category: Deisenhofer, J.]] | [[Category: Deisenhofer, J.]] | ||
[[Category: atp binding]] | [[Category: atp binding]] | ||
[[Category: atp grasp]] | [[Category: atp grasp]] | ||
[[Category: calcium (ii) ion]] | [[Category: calcium (ii) ion]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:05:43 2008'' | ||
Revision as of 20:05, 30 March 2008
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| 1px2, resolution 2.23Å | |||||||||||||
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| Ligands: | ATP, CA | ||||||||||||
| Gene: | SYN1 (Rattus norvegicus) | ||||||||||||
| Related: | 1PK8, 1AUX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)
Overview
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.
About this Structure
1PX2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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