Download MendeleyStructure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, at 2.4 A resolution: a putative member of the StAR-related lipid-transfer (START) domain superfamily.
Nakabayashi, M., Shibata, N., Komori, H., Ueda, Y., Iino, H., Ebihara, A., Kuramitsu, S., Higuchi, Y.(2005) Acta Crystallogr Sect F Struct Biol Cryst Commun 61: 1027-1031
- PubMed: 16511226
- DOI: https://doi.org/10.1107/S1744309105035372
- Primary Citation of Related Structures:
2D4R - PubMed Abstract:
The crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 A resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact alpha+beta motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules.
Organizational Affiliation:
Department of Life Science, Graduate School of Life Science, University of Hyogo, Himeji Institute of Technology, 3-2-1 Koto, Ako-gun, Hyogo 678-1297, Japan.
