1px2 | pdb_00001px2
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 with CA and ATP as ligands. 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
Page seeded by OCA on Wed Nov 21 00:11:48 2007
