Structure of the Thermus thermophilus putative periplasmic glutamate/glutamine-binding protein

Hitomi Takahashi, Eiji Inagaki, Chizu Kuroishi, Tahir H. Tahirov

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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 Å using the multiple-wavelength anomalous dispersion (MAD) method and a selenomethionine-incorporated protein. The native protein structure was solved to 1.5 Å 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.

Original languageEnglish (US)
Pages (from-to)1846-1854
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Issue number10
StatePublished - Oct 2004
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology


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