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
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.
Structure 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 Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt, 12):1027-31. Epub 2005 Nov 5. PMID:16511226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakabayashi M, Shibata N, Komori H, Ueda Y, Iino H, Ebihara A, Kuramitsu S, Higuchi Y. Structure 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. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt, 12):1027-31. Epub 2005 Nov 5. PMID:16511226 doi:http://dx.doi.org/10.1107/S1744309105035372
