2nnz | pdb_00002nnz

Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus

spinqualitylabelsall models 2nnz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nnz is a 1 chain structure with sequence from Archaeoglobus fulgidus DSM 4304. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O28042_ARCFU 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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