1auv
From Proteopedia
(New page: 200px<br /><applet load="1auv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1auv, resolution 2.15Å" /> '''STRUCTURE OF THE C D...) |
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| - | [[Image:1auv.gif|left|200px]]<br /><applet load="1auv" size=" | + | [[Image:1auv.gif|left|200px]]<br /><applet load="1auv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1auv, resolution 2.15Å" /> | caption="1auv, resolution 2.15Å" /> | ||
'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN'''<br /> | '''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Synapsins are abundant synaptic vesicle proteins with an essential | + | Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1AUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1AUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: synapsin ia c-domain]] | [[Category: synapsin ia c-domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:32 2008'' |
Revision as of 09:48, 21 February 2008
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STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN
Overview
Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.
About this Structure
1AUV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Synapsin I is structurally similar to ATP-utilizing enzymes., Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J, EMBO J. 1998 Feb 16;17(4):977-84. PMID:9463376
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