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New page: left|200px<br /><applet load="1iit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iit, resolution 1.90Å" /> '''GLUR0 LIGAND BINDING...
 
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[[Image:1iit.gif|left|200px]]<br /><applet load="1iit" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iit, resolution 1.90&Aring;" />
'''GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE'''<br />


==Overview==
==GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE==
High-resolution structures of the ligand binding core of GluR0, a, glutamate receptor ion channel from Synechocystis PCC 6803, have been, solved by X-ray diffraction. The GluR0 structures reveal homology with, bacterial periplasmic binding proteins and the rat GluR2 AMPA subtype, neurotransmitter receptor. The ligand binding site is formed by a cleft, between two globular alpha/beta domains. L-Glutamate binds in an extended, conformation, similar to that observed for glutamine binding protein, (GlnBP). However, the L-glutamate gamma-carboxyl group interacts, exclusively with Asn51 in domain 1, different from the interactions of, ligand with domain 2 residues observed for GluR2 and GlnBP. To address how, neutral amino acids activate GluR0 gating we solved the structure of the, binding site complex with L-serine. This revealed solvent molecules acting, as surrogate ligand atoms, such that the serine OH group makes, solvent-mediated hydrogen bonds with Asn51. The structure of a, ligand-free, closed-cleft conformation revealed an extensive hydrogen bond, network mediated by solvent molecules. Equilibrium centrifugation analysis, revealed dimerization of the GluR0 ligand binding core with a dissociation, constant of 0.8 microM. In the crystal, a symmetrical dimer involving, residues in domain 1 occurs along a crystallographic 2-fold axis and, suggests that tetrameric glutamate receptor ion channels are assembled, from dimers of dimers. We propose that ligand-induced conformational, changes cause the ion channel to open as a result of an increase in domain, 2 separation relative to the dimer interface.
<StructureSection load='1iit' size='340' side='right'caption='[[1iit]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IIT 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SER:SERINE'>SER</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=1iit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iit OCA], [https://pdbe.org/1iit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iit RCSB], [https://www.ebi.ac.uk/pdbsum/1iit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iit ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P73797_SYNY3 P73797_SYNY3]
== 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/ii/1iit_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=1iit ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with SER as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IIT OCA].
*[[Glutamate receptor (GluA2)|Glutamate receptor (GluA2)]]
 
__TOC__
==Reference==
</StructureSection>
Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state., Mayer ML, Olson R, Gouaux E, J Mol Biol. 2001 Aug 24;311(4):815-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11518533 11518533]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
[[Category: Synechocystis sp.]]
[[Category: Gouaux E]]
[[Category: Gouaux, E.]]
[[Category: Mayer ML]]
[[Category: Mayer, M.L.]]
[[Category: Olson R]]
[[Category: Olson, R.]]
[[Category: SER]]
[[Category: membrane protein]]
[[Category: same fold as pbps]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:25:52 2007''

Latest revision as of 07:36, 7 February 2024

GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE

1iit, resolution 1.90Å

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