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1yw5

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[[Image:1yw5.gif|left|200px]]<br /><applet load="1yw5" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yw5, resolution 1.60&Aring;" />
 
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'''Peptidyl-prolyl isomerase ESS1 from Candida albicans'''<br />
 
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==Overview==
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==Peptidyl-prolyl isomerase ESS1 from Candida albicans==
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Ess1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that binds to the carboxy-terminal domain (CTD) of RNA polymerase II. Ess1 is thought to function by inducing conformational changes in the CTD that control the assembly of cofactor complexes on the transcription unit. Ess1 (also called Pin1) is highly conserved throughout the eukaryotic kingdom and is required for growth in some species, including the human fungal pathogen Candida albicans. Here we report the crystal structure of the C. albicansEss1 protein, determined at 1.6 A resolution. The structure reveals two domains, the WW and the isomerase domain, that have conformations essentially identical to those of human Pin1. However, the linker region that joins the two domains is quite different. In human Pin1, this linker is short and flexible, and part of it is unstructured. In contrast, the fungal Ess1 linker is highly ordered and contains a long alpha-helix. This structure results in a rigid juxtaposition of the WW and isomerase domains, in an orientation that is distinct from that observed in Pin1, and that eliminates a hydrophobic pocket between the domains that was implicated as the main substrate recognition site. These differences suggest distinct modes of interaction with long substrate molecules, such as the CTD of RNA polymerase II. We also show that C. albicans ess1(-)() mutants are attenuated for in vivo survival in mice. Together, these results suggest that CaEss1 might constitute a useful antifungal drug target, and that structural differences between the fungal and human enzymes could be exploited for drug design.
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<StructureSection load='1yw5' size='340' side='right'caption='[[1yw5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yw5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YW5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=1yw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yw5 OCA], [https://pdbe.org/1yw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yw5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q59KZ2_CANAL Q59KZ2_CANAL]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yw/1yw5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1yw5 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1YW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YW5 OCA].
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility., Li Z, Li H, Devasahayam G, Gemmill T, Chaturvedi V, Hanes SD, Van Roey P, Biochemistry. 2005 Apr 26;44(16):6180-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15835905 15835905]
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[[Category: Candida albicans]]
[[Category: Candida albicans]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chaturvedi V]]
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[[Category: Chaturvedi, V.]]
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[[Category: Devasahayam G]]
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[[Category: Devasahayam, G.]]
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[[Category: Gemmill T]]
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[[Category: Gemmill, T.]]
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[[Category: Hanes SD]]
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[[Category: Hanes, S D.]]
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[[Category: Li H]]
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[[Category: Li, H.]]
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[[Category: Li Z]]
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[[Category: Li, Z.]]
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[[Category: Van Roey P]]
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[[Category: Roey, P Van.]]
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[[Category: ordered linker]]
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[[Category: ppiase domain]]
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[[Category: ww-domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:56 2008''
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Current revision

Peptidyl-prolyl isomerase ESS1 from Candida albicans

PDB ID 1yw5

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