2NNZ

Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus

Summary for 2NNZ

• Entry DOI: 10.2210/pdb2nnz/pdb
• NMR Information: BMRB: 7271
• Descriptor: Hypothetical protein (1 entity in total)
• Functional Keywords: beta-barrel, structural genomics, ontario centre for structural proteomics, ocsp, unknown function
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 1
• Total formula weight: 17135.25

Authors

Ai, X.,Semesib, A.,Yee, A.,Arrowsmith, C.H.,Li, S.S.C.,Choy, W.Y.,Ontario Centre for Structural Proteomics (OCSP) (deposition date: 2006-10-24, release date: 2007-08-28, Last modification date: 2024-05-15)

Primary citation

Ai, X.,Li, L.,Semesi, A.,Yee, A.,Arrowsmith, C.H.,Li, S.S.,Choy, W.Y.
Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold.
J.Biomol.Nmr, 38:353-358, 2007

PubMed 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 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.

PubMed: 17610131
DOI: 10.1007/s10858-007-9172-8

Experimental method

SOLUTION NMR