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==Crystal structure of yeast cyclophilin A, CPR1== | ==Crystal structure of yeast cyclophilin A, CPR1== | ||
<StructureSection load='1ist' size='340' side='right' caption='[[1ist]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1ist' size='340' side='right'caption='[[1ist]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ist]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ist]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IST FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ist FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ist OCA], [https://pdbe.org/1ist PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ist RCSB], [https://www.ebi.ac.uk/pdbsum/1ist PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ist ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CYPH_YEAST CYPH_YEAST] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles.<ref>PMID:11641409</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/1ist_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/1ist_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1ist ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Cyclophilin|Cyclophilin]] | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Kashima | [[Category: Kashima A]] | ||
[[Category: Konno | [[Category: Konno M]] | ||
[[Category: Yoshikawa-Fujioka | [[Category: Yoshikawa-Fujioka S]] | ||
Latest revision as of 02:36, 28 December 2023
Crystal structure of yeast cyclophilin A, CPR1Crystal structure of yeast cyclophilin A, CPR1
Structural highlights
FunctionCYPH_YEAST PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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