1ii5: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ii5.gif|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE GLUR0 LIGAND BINDING CORE COMPLEX WITH L-GLUTAMATE==
-The line below this paragraph, containing "STRUCTURE_1ii5", creates the "Structure Box" on the page.
+<StructureSection load='1ii5' size='340' side='right'caption='[[1ii5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ii5]] 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=1II5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1II5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr>
-{{STRUCTURE_1ii5|  PDB=1ii5  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ii5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii5 OCA], [https://pdbe.org/1ii5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ii5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ii5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ii5 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/1ii5_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=1ii5 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF THE GLUR0 LIGAND BINDING CORE COMPLEX WITH L-GLUTAMATE'''
+==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]]
-II5 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=1II5 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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:01:49 2008''