1us4

From Proteopedia

Revision as of 11:51, 30 October 2007

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 ... [(full description)]

About 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].

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

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