1aux: Difference between revisions

Line 1:

~~{{STRUCTURE_1aux| PDB=1aux | SCENE= }}~~

==STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND==

===STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND===

~~{{ABSTRACT_PUBMED_9463376}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[1aux]] is a 2 chain structure with 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=1AUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUX FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aux RCSB], [http://www.ebi.ac.uk/pdbsum/1aux PDBsum]</span></td></tr>

<table>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aux_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>

<text>to colour the structure by Evolutionary Conservation</text>

</jmolCheckbox>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

== Publication Abstract from PubMed ==

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.

~~==Function==~~

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<ref>PMID:9463376</ref>

~~[[http://www~~.~~uniprot.org/uniprot/SYN1_BOVIN SYN1_BOVIN]] Neuronal phosphoprotein that coats synaptic vesicles~~, ~~binds to the cytoskeleton~~, ~~and is believed to function in the regulation of neurotransmitter release~~. ~~The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level~~ (~~By similarity~~).

~~==About this Structure==~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[1aux]] is~~ a ~~2 chain structure with 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=1AUX OCA].~~

</div>

== References ==

==~~Reference~~==

~~<ref group="xtra">PMID:009463376</ref>~~<references ~~group="xtra"~~/><~~references~~/>

__TOC__

</StructureSection>

[[Category: Bos taurus]]

[[Category: Deisenhofer, J.]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1aux|  PDB=1aux  |  SCENE=  }}
+==STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND==
-===STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND===
+<StructureSection load='1aux' size='340' side='right' caption='[[1aux]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-{{ABSTRACT_PUBMED_9463376}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1aux]] is a 2 chain structure with 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=1AUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUX FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aux RCSB], [http://www.ebi.ac.uk/pdbsum/1aux PDBsum]</span></td></tr>
+<table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aux_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Function==
+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<ref>PMID:9463376</ref>
-[[http://www.uniprot.org/uniprot/SYN1_BOVIN SYN1_BOVIN]] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity).
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[1aux]] is a 2 chain structure with 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=1AUX OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:009463376</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
 [[Category: Deisenhofer, J.]]