1yw5
From Proteopedia
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| - | [[Image:1yw5.gif|left|200px]] | + | [[Image:1yw5.gif|left|200px]] |
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| - | '''Peptidyl-prolyl isomerase ESS1 from Candida albicans''' | + | {{Structure |
| + | |PDB= 1yw5 |SIZE=350|CAPTION= <scene name='initialview01'>1yw5</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Peptidyl-prolyl isomerase ESS1 from Candida albicans''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YW5 is a [ | + | 1YW5 is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/15835905 15835905] |
[[Category: Candida albicans]] | [[Category: Candida albicans]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: ww-domain]] | [[Category: ww-domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:14 2008'' |
Revision as of 13:28, 20 March 2008
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| , resolution 1.60Å | |||||||
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| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Peptidyl-prolyl isomerase ESS1 from Candida albicans
Overview
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.
About this Structure
1YW5 is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.
Reference
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:15835905
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