Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takahashi H, Inagaki E, Kuroishi C, Tahirov TH. Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1846-54. Epub 2004, Sep 23. PMID:15388932 doi:10.1107/S0907444904019420
