1pk8

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[[Image:1pk8.gif|left|200px]]
[[Image:1pk8.gif|left|200px]]
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{{Structure
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|PDB= 1pk8 |SIZE=350|CAPTION= <scene name='initialview01'>1pk8</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1pk8", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|GENE= SYN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=
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{{STRUCTURE_1pk8| PDB=1pk8 | SCENE= }}
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|RELATEDENTRY=[[1aux|1AUX]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pk8 OCA], [http://www.ebi.ac.uk/pdbsum/1pk8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pk8 RCSB]</span>
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'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP'''
'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP'''
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[[Category: Chelliah, Y.]]
[[Category: Chelliah, Y.]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: atp binding]]
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[[Category: Atp binding]]
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[[Category: atp grasp]]
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[[Category: Atp grasp]]
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[[Category: calcium (ii) ion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:10:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:51 2008''
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Revision as of 02:10, 3 May 2008

Image:1pk8.gif

Template:STRUCTURE 1pk8

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP


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

1PK8 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 Page seeded by OCA on Sat May 3 05:10:57 2008

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