1aux: Difference between revisions

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[[Image:1aux.gif|left|200px]]<br /><applet load="1aux" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1aux.gif|left|200px]]<br /><applet load="1aux" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1aux, resolution 2.30Å" />

'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND'''<br />

==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.

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==

1AUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and SAP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].

1AUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SAP:'>SAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].

==Reference==

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[[Category: synapsin ia c-domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:08:~~49 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:31 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1aux.gif|left|200px]]<br /><applet load="1aux" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1aux.gif|left|200px]]<br /><applet load="1aux" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1aux, resolution 2.30&Aring;" />
 '''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND'''<br />
 ==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.
+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==
-AUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and SAP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].
+AUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SAP:'>SAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: synapsin ia c-domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:08:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:31 2008''