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1iit

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[[Image:1iit.gif|left|200px]]
 
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{{Structure
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==GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE==
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|PDB= 1iit |SIZE=350|CAPTION= <scene name='initialview01'>1iit</scene>, resolution 1.90&Aring;
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<StructureSection load='1iit' size='340' side='right'caption='[[1iit]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SER:SERINE'>SER</scene>
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<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>
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|ACTIVITY=
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</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>
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|GENE= slr1257 GluR0 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
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<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>
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}}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P73797_SYNY3 P73797_SYNY3]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ii/1iit_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1iit ConSurf].
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<div style="clear:both"></div>
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'''GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE'''
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==See Also==
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*[[Glutamate receptor (GluA2)|Glutamate receptor (GluA2)]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
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==About this Structure==
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[[Category: Gouaux E]]
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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].
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[[Category: Mayer ML]]
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[[Category: Olson R]]
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==Reference==
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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]
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[[Category: Single protein]]
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[[Category: Synechocystis sp.]]
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[[Category: Gouaux, E.]]
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[[Category: Mayer, M L.]]
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[[Category: Olson, R.]]
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[[Category: SER]]
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[[Category: membrane protein]]
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[[Category: same fold as pbp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:57 2008''
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Current revision

GLUR0 LIGAND BINDING CORE COMPLEX WITH L-SERINE

PDB ID 1iit

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