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
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 beta-barrel core composed of eight beta-strands, one alpha-helix, and one 3(10) 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.
Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold.,Ai X, Li L, Semesi A, Yee A, Arrowsmith CH, Li SS, Choy WY J Biomol NMR. 2007 Aug;38(4):353-8. Epub 2007 Jul 4. PMID:17610131[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ai X, Li L, Semesi A, Yee A, Arrowsmith CH, Li SS, Choy WY. Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold. J Biomol NMR. 2007 Aug;38(4):353-8. Epub 2007 Jul 4. PMID:17610131 doi:10.1007/s10858-007-9172-8
