2nnz
From Proteopedia
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| - | [[Image:2nnz.jpg|left|200px]] | ||
| - | < | + | ==Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus== |
| - | + | <StructureSection load='2nnz' size='340' side='right'caption='[[2nnz]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2nnz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNZ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnz OCA], [https://pdbe.org/2nnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnz RCSB], [https://www.ebi.ac.uk/pdbsum/2nnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnz ProSAT]</span></td></tr> | |
| - | --> | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/O28042_ARCFU O28042_ARCFU] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | == | + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/2nnz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nnz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | 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<ref>PMID:17610131</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Archaeoglobus fulgidus]] | + | <div class="pdbe-citations 2nnz" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Ai | + | <references/> |
| - | [[Category: Arrowsmith | + | __TOC__ |
| - | [[Category: Choy | + | </StructureSection> |
| - | [[Category: Li | + | [[Category: Archaeoglobus fulgidus DSM 4304]] |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: Semesib | + | [[Category: Ai X]] |
| - | [[Category: Yee | + | [[Category: Arrowsmith CH]] |
| - | + | [[Category: Choy WY]] | |
| - | + | [[Category: Li SSC]] | |
| - | + | [[Category: Semesib A]] | |
| - | + | [[Category: Yee A]] | |
| - | + | ||
| - | + | ||
Current revision
Solution structure of the hypothetical protein AF2241 from Archaeoglobus fulgidus
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