1iiw
From Proteopedia
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'''GLUR0 LIGAND BINDING CORE: CLOSED-CLEFT LIGAND-FREE STRUCTURE''' | '''GLUR0 LIGAND BINDING CORE: CLOSED-CLEFT LIGAND-FREE STRUCTURE''' | ||
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[[Category: Mayer, M L.]] | [[Category: Mayer, M L.]] | ||
[[Category: Olson, R.]] | [[Category: Olson, R.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:03:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:03, 2 May 2008
GLUR0 LIGAND BINDING CORE: CLOSED-CLEFT LIGAND-FREE STRUCTURE
Overview
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.
About this Structure
1IIW is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
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:11518533 Page seeded by OCA on Fri May 2 20:03:09 2008
