Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold |
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Authors: | Xuanjun Ai Lei Li Anthony Semesi Adelinda Yee Cheryl H Arrowsmith Shawn S C Li Wing-Yiu Choy |
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Institution: | (1) Department of Biochemistry, The University of Western Ontario, London, ON, Canada, N6A 5C1;(2) Ontario Centre for Structural Proteomics, University Health Network, Toronto, ON, Canada, M5G 2C4 |
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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.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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Keywords: | Archaeoglobus fulgidus Cyclophilin-like fold DUF369 domain NMR Protein structure Structural proteomics |
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