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- Title
Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein.
- Authors
Takahashi, Hitomi; Inagaki, Eiji; Kuroishi, Chizu; Tahirov, Tahir H
- 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.
- Publication
Acta crystallographica. Section D, Biological crystallography, 2004, Vol 60, Issue Pt 10, p1846
- ISSN
0907-4449
- Publication type
Journal Article
- DOI
10.1107/S0907444904019420