1pk8

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(New page: 200px<br /><applet load="1pk8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pk8, resolution 2.1&Aring;" /> '''Crystal Structure of ...)
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caption="1pk8, resolution 2.1&Aring;" />
'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP'''<br />
'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1PK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA, ATP and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PK8 OCA].
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1PK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PK8 OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brautigam, C.A.]]
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[[Category: Brautigam, C A.]]
[[Category: Chelliah, Y.]]
[[Category: Chelliah, Y.]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: calcium (ii) ion]]
[[Category: calcium (ii) ion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:53:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:42 2008''

Revision as of 12:29, 21 February 2008

Image:1pk8.gif

1pk8, resolution 2.1Å

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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 with , and 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

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