1US5

PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE

Summary for 1US5

• Entry DOI: 10.2210/pdb1us5/pdb
• Related: 1US4
• Descriptor: PUTATIVE GLUR0 LIGAND BINDING CORE, GLUTAMIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: receptor, membrane protein, glutamate receptor, glur0, l-glutamate, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 1
• Total formula weight: 33697.89

Authors

Tahirov, T.H.,Inagaki, E. (deposition date: 2003-11-18, release date: 2003-11-19, Last modification date: 2023-12-13)

Primary citation

Takahashi, H.,Inagaki, E.,Kuroishi, C.,Tahirov, T.H.
Structure of the Thermus Thermophilus Putative Periplasmic Glutamate/Glutamine-Binding Protein
Acta Crystallogr.,Sect.D, 60:1846-, 2004

PubMed Abstract: 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.

PubMed: 15388932
DOI: 10.1107/S0907444904019420

Experimental method

X-RAY DIFFRACTION (1.5 Å)