1us4
From Proteopedia
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|PDB= 1us4 |SIZE=350|CAPTION= <scene name='initialview01'>1us4</scene>, resolution 1.75Å | |PDB= 1us4 |SIZE=350|CAPTION= <scene name='initialview01'>1us4</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=EGL:GLU+Binding+Site+For+Chain+A'>EGL</scene> | |SITE= <scene name='pdbsite=EGL:GLU+Binding+Site+For+Chain+A'>EGL</scene> | ||
| - | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1us4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us4 OCA], [http://www.ebi.ac.uk/pdbsum/1us4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1us4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tahirov, T H.]] | [[Category: Tahirov, T H.]] | ||
[[Category: Takahashi, H.]] | [[Category: Takahashi, H.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: GLU]] | ||
[[Category: glur0]] | [[Category: glur0]] | ||
[[Category: glutamate receptor]] | [[Category: glutamate receptor]] | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:27 2008'' |
Revision as of 21:14, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE
Overview
As part of a structural genomics project, the crystal structure of a 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was solved to 1.75 A using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 A using the molecular-replacement method. Both structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold related to the periplasmic substrate-binding proteins (PSBP). Further comparative structural analysis with other PSBP-fold proteins revealed the conservation of the predicted membrane permease binding surface area and indicated that the T. thermophilus HB8 molecule is most likely to be an L-glutamate and/or an L-glutamine-binding protein related to the cluster 3 periplasmic receptors. However, the geometry of ligand binding is unique to the T. thermophilus HB8 molecule.
About this Structure
1US4 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein., Takahashi H, Inagaki E, Kuroishi C, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1846-54. Epub 2004, Sep 23. PMID:15388932
Page seeded by OCA on Mon Mar 31 00:14:27 2008
