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.
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.
Nakabayashi
Makoto
M
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.
Shibata
Naoki
N
Komori
Hirofumi
H
Ueda
Yasufumi
Y
Iino
Hitoshi
H
Ebihara
Akio
A
Kuramitsu
Seiki
S
Higuchi
Yoshiki
Y
D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism; D006860:Hydrogen Bonding; D008024:Ligands; D026901:Membrane Transport Proteins / Q000737:chemistry*; D008958:Models, Molecular; D005810:Multigene Family; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016963:Thermus thermophilus / Q000378:metabolism*; D014961:X-Ray Diffraction
D008024:Ligands; D026901:Membrane Transport Proteins