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2nnz

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[[Image:2nnz.jpg|left|200px]]
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{{Structure
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|GENE= AF2241 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
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{{STRUCTURE_2nnz| PDB=2nnz | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnz OCA], [http://www.ebi.ac.uk/pdbsum/2nnz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nnz RCSB]</span>
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'''Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus'''
'''Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus'''
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Revision as of 06:41, 4 May 2008

Image:2nnz.jpg

Template:STRUCTURE 2nnz

Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus


Overview

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.

About this Structure

2NNZ is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 09:41:20 2008

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