3bt8
From Proteopedia
(Difference between revisions)
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<StructureSection load='3bt8' size='340' side='right'caption='[[3bt8]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3bt8' size='340' side='right'caption='[[3bt8]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bt8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3bt8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BT8 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bt8 OCA], [https://pdbe.org/3bt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bt8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bt8 ProSAT]</span></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=3bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bt8 OCA], [https://pdbe.org/3bt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bt8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bt8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3bt8 ConSurf]. | </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=3bt8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail. | ||
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| - | Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.,Venugopal V, Sen B, Datta AK, Banerjee R Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):60-4. Epub 2007 Jan 17. PMID:17277440<ref>PMID:17277440</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3bt8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Leishmania donovani]] |
| - | + | [[Category: Banerjee R]] | |
| - | [[Category: Banerjee | + | [[Category: Datta AK]] |
| - | [[Category: Datta | + | [[Category: Sen B]] |
| - | [[Category: Sen | + | [[Category: Venugopal V]] |
| - | [[Category: Venugopal | + | |
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Current revision
Crystal Structure of Mutant Cyclophilin (R147A) from Leishmania donovani
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