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1auv: Difference between revisions

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<StructureSection load='1auv' size='340' side='right'caption='[[1auv]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='1auv' size='340' side='right'caption='[[1auv]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1auv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1auv]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUV FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auv OCA], [https://pdbe.org/1auv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auv RCSB], [https://www.ebi.ac.uk/pdbsum/1auv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auv OCA], [https://pdbe.org/1auv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auv RCSB], [https://www.ebi.ac.uk/pdbsum/1auv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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).  
[https://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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=1auv ConSurf].
</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/main_output.php?pdb_ID=1auv ConSurf].
<div style="clear:both"></div>
<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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1auv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Synapsin|Synapsin]]
*[[Synapsin|Synapsin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Deisenhofer, J]]
[[Category: Deisenhofer J]]
[[Category: Esser, L]]
[[Category: Esser L]]
[[Category: Wang, C]]
[[Category: Wang C]]
[[Category: Phosphorylation]]
[[Category: Synapse]]
[[Category: Synapsin ia c-domain]]
[[Category: Transferase]]

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