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[[Image:1w15.gif|left|200px]]


{{Structure
==rat synaptotagmin 4 C2B domain in the presence of calcium==
|PDB= 1w15 |SIZE=350|CAPTION= <scene name='initialview01'>1w15</scene>, resolution 1.93&Aring;
<StructureSection load='1w15' size='340' side='right'caption='[[1w15]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
<table><tr><td colspan='2'>[[1w15]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W15 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w15 OCA], [https://pdbe.org/1w15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w15 RCSB], [https://www.ebi.ac.uk/pdbsum/1w15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w15 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w15 OCA], [http://www.ebi.ac.uk/pdbsum/1w15 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w15 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/SYT4_RAT SYT4_RAT] Synaptotagmin family member which does not bind Ca(2+) (PubMed:7993622). Involved in neuronal dense core vesicles (DCVs) mobility through its interaction with KIF1A. Upon increased neuronal activity, phosphorylation by MAPK8/JNK1 destabilizes the interaction with KIF1A and captures DCVs to synapses (PubMed:29166604). Plays a role in dendrite formation by melanocytes (By similarity).[UniProtKB:Q9H2B2]<ref>PMID:29166604</ref> <ref>PMID:7993622</ref>
== 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/w1/1w15_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/main_output.php?pdb_ID=1w15 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The neuronal protein synaptotagmin 1 functions as a Ca(2+) sensor in exocytosis via two Ca(2+)-binding C(2) domains. The very similar synaptotagmin 4, which includes all the predicted Ca(2+)-binding residues in the C(2)B domain but not in the C(2)A domain, is also thought to function as a neuronal Ca(2+) sensor. Here we show that, unexpectedly, both C(2) domains of fly synaptotagmin 4 exhibit Ca(2+)-dependent phospholipid binding, whereas neither C(2) domain of rat synaptotagmin 4 binds Ca(2+) or phospholipids efficiently. Crystallography reveals that changes in the orientations of critical Ca(2+) ligands, and perhaps their flexibility, render the rat synaptotagmin 4 C(2)B domain unable to form full Ca(2+)-binding sites. These results indicate that synaptotagmin 4 is a Ca(2+) sensor in the fly but not in the rat, that the Ca(2+)-binding properties of C(2) domains cannot be reliably predicted from sequence analyses, and that proteins clearly identified as orthologs may nevertheless have markedly different functional properties.


'''RAT SYNAPTOTAGMIN 4 C2B DOMAIN IN THE PRESENCE OF CALCIUM'''
Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4.,Dai H, Shin OH, Machius M, Tomchick DR, Sudhof TC, Rizo J Nat Struct Mol Biol. 2004 Sep;11(9):844-9. Epub 2004 Aug 15. PMID:15311271<ref>PMID:15311271</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1w15" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The neuronal protein synaptotagmin 1 functions as a Ca(2+) sensor in exocytosis via two Ca(2+)-binding C(2) domains. The very similar synaptotagmin 4, which includes all the predicted Ca(2+)-binding residues in the C(2)B domain but not in the C(2)A domain, is also thought to function as a neuronal Ca(2+) sensor. Here we show that, unexpectedly, both C(2) domains of fly synaptotagmin 4 exhibit Ca(2+)-dependent phospholipid binding, whereas neither C(2) domain of rat synaptotagmin 4 binds Ca(2+) or phospholipids efficiently. Crystallography reveals that changes in the orientations of critical Ca(2+) ligands, and perhaps their flexibility, render the rat synaptotagmin 4 C(2)B domain unable to form full Ca(2+)-binding sites. These results indicate that synaptotagmin 4 is a Ca(2+) sensor in the fly but not in the rat, that the Ca(2+)-binding properties of C(2) domains cannot be reliably predicted from sequence analyses, and that proteins clearly identified as orthologs may nevertheless have markedly different functional properties.
*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1W15 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W15 OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural basis for the evolutionary inactivation of Ca2+ binding to synaptotagmin 4., Dai H, Shin OH, Machius M, Tomchick DR, Sudhof TC, Rizo J, Nat Struct Mol Biol. 2004 Sep;11(9):844-9. Epub 2004 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15311271 15311271]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Dai H]]
[[Category: Dai, H.]]
[[Category: Machius M]]
[[Category: Machius, M.]]
[[Category: Rizo J]]
[[Category: Rizo, J.]]
[[Category: Shin O-H]]
[[Category: Shin, O H.]]
[[Category: Sudhof TC]]
[[Category: Sudhof, T C.]]
[[Category: Tomchick DR]]
[[Category: Tomchick, D R.]]
[[Category: calcium]]
[[Category: endocytosis/exocytosis]]
[[Category: neurotransmitter release]]
[[Category: synaptotagmin]]
[[Category: transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:42 2008''

Latest revision as of 13:11, 13 December 2023

rat synaptotagmin 4 C2B domain in the presence of calcium

1w15, resolution 1.93Å

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