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| {{STRUCTURE_1px2| PDB=1px2 | SCENE= }} | | {{STRUCTURE_1px2| PDB=1px2 | SCENE= }} |
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| '''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)'''
| | ===Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14688264}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14688264 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14688264}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Atp binding]] | | [[Category: Atp binding]] |
| [[Category: Atp grasp]] | | [[Category: Atp grasp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:35:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:39:20 2008'' |
