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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.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2005 Dec 01; Vol. 61 (Pt 12), pp. 1027-31. Date of Electronic Publication: 2005 Nov 05. - Publication Year :
- 2005
-
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.
- Subjects :
- Escherichia coli metabolism
Hydrogen Bonding
Ligands
Models, Molecular
Multigene Family
Protein Binding
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
X-Ray Diffraction
Crystallography, X-Ray methods
Membrane Transport Proteins chemistry
Thermus thermophilus metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 61
- Issue :
- Pt 12
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 16511226
- Full Text :
- https://doi.org/10.1107/S1744309105035372