Abstract
AF2241 is a hypothetical protein from Archaeoglobus fulgidus and it belongs to the PFam domain of unknown function 369 (DUF369). NMR structural determination reveals that AF2241 adopts a cyclophilin-like fold, with a β-barrel core composed of eight β-strands, one α-helix, and one 310 helix located at each end of the barrel. The protein displays a high structural similarity to TM1367, another member of DUF369 whose structure has been determined recently by X-ray crystallography. Structural similarity search shows that AF2241 also has a high similarity to human cyclophilin A, however, sequence alignment and electrostatic potential analysis reveal that the residues in the PPIase catalytic site of human cyclophilin A are not conserved in AF2241 or TM1367. Instead, a putative active site of AF2241 maps to a negatively charged pocket composed of 9 conserved residues. Our results suggest that although AF2241 adopts the same fold as the human cyclophilin A, it may have distinct biological function.
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Acknowledgements
We would like to thank Drs. Hsiu-Ju Tseng and Matthew Revington for helpful discussions. This work was supported by the Ontario Research Development Challenge Fund (to CHA and SSCL), Genome Canada, and a CIHR resource Grant.
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Ai, X., Li, L., Semesi, A. et al. Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold. J Biomol NMR 38, 353–358 (2007). https://doi.org/10.1007/s10858-007-9172-8
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DOI: https://doi.org/10.1007/s10858-007-9172-8