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


{{Structure
==GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE==
|PDB= 1iit |SIZE=350|CAPTION= <scene name='initialview01'>1iit</scene>, resolution 1.90&Aring;
<StructureSection load='1iit' size='340' side='right'caption='[[1iit]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SER:SERINE'>SER</scene>
<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>
|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]] 1.9&#8491;</td></tr>
|GENE= slr1257 GluR0 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1iiw|1IIW]], [[1ii5|1II5]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iit OCA], [http://www.ebi.ac.uk/pdbsum/1iit PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iit RCSB]</span>
== 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>


'''GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE'''
==See Also==
 
*[[Glutamate receptor (GluA2)|Glutamate receptor (GluA2)]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
==About this Structure==
[[Category: Gouaux E]]
1IIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIT OCA].
[[Category: Mayer ML]]
 
[[Category: Olson R]]
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/11518533 11518533]
[[Category: Single protein]]
[[Category: Synechocystis sp.]]
[[Category: Gouaux, E.]]
[[Category: Mayer, M L.]]
[[Category: Olson, R.]]
[[Category: membrane protein]]
[[Category: same fold as pbp]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:22 2008''

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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