1us4
|
PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE
OverviewOverview
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 StructureAbout this Structure
1US4 is a Single protein structure of sequence from Thermus thermophilus with GLU and EDO as ligands. Structure known Active Site: EGL. Full crystallographic information is available from OCA.
ReferenceReference
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 Nov 5 15:05:21 2007