1px2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1px2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1px2, resolution 2.23Å" /> '''Crystal Structure of...
 
OCA (talk | contribs)
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1px2.jpg|left|200px]]<br /><applet load="1px2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1px2, resolution 2.23&Aring;" />
'''Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)'''<br />


==Overview==
==Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)==
Synapsins are multidomain proteins that are critical for regulating, neurotransmitter release in vertebrates. In the present study, two crystal, structures of the C domain of rat synapsin I (rSynI-C) in complex with, Ca(2+) and ATP reveal that this protein can form a tetramer and that a, flexible loop (the "multifunctional loop") contacts bound ATP. Further, experiments were carried out on a protein comprising the A, B, and C, domains of rat synapsin I (rSynI-ABC). An ATP-stabilized tetramer of, rSynI-ABC is observed during velocity sedimentation and size-exclusion, chromatographic experiments. These hydrodynamic results also indicate that, the A and B domains exist in an extended conformation. Calorimetric, measurements of ATP binding to wild-type and mutant rSynI-ABC demonstrate, that the multifunctional loop and a cross-tetramer contact are important, for ATP binding. The evidence supports a view of synapsin I as an, ATP-utilizing, tetrameric protein made up of monomers that have a, flexible, extended N terminus.
<StructureSection load='1px2' size='340' side='right'caption='[[1px2]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1px2]] is a 2 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=1PX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PX2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1px2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px2 OCA], [https://pdbe.org/1px2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1px2 RCSB], [https://www.ebi.ac.uk/pdbsum/1px2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1px2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYN1_RAT SYN1_RAT] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.
== 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/px/1px2_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=1px2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1PX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PX2 OCA].
*[[Synapsin|Synapsin]]
 
__TOC__
==Reference==
</StructureSection>
Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I., Brautigam CA, Chelliah Y, Deisenhofer J, J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14688264 14688264]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Brautigam CA]]
[[Category: Brautigam, C.A.]]
[[Category: Chelliah Y]]
[[Category: Chelliah, Y.]]
[[Category: Deisenhofer J]]
[[Category: Deisenhofer, J.]]
[[Category: ATP]]
[[Category: CA]]
[[Category: atp binding]]
[[Category: atp grasp]]
[[Category: calcium (ii) ion]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:11:48 2007''

Latest revision as of 13:28, 13 March 2024

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)

1px2, resolution 2.23Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA