ArticleBiochemistry2005
The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Coevolution of the Ess1-CTD axis in polar fungi suggests a role for phase separation in cold tolerance.Science advances · 2022Article
- Antifungal Activity ofInternational journal of molecular sciences · 2021Article
- What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domainRSC chemical biology · 2021Review
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Allostery and Epistasis: Emergent Properties of Anisotropic Networks.Entropy (Basel, Switzerland) · 2020Article
- Genetic interactions and transcriptomics implicate fission yeast CTD prolyl isomerase Pin1 as an agent of RNA 3' processing and transcription termination that functions via its effects on CTD phosphatase Ssu72.Nucleic acids research · 2020Article
- NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.BMC biology · 2016Article
- Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Journal of biological chemistry · 2015Article
- The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.G3 (Bethesda, Md.) · 2014Article
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- Role of Ess1 in growth, morphogenetic switching, and RNA polymerase II transcription in Candida albicans.PloS one · 2013Article
- Structural and kinetic analysis of prolyl-isomerization/phosphorylation cross-talk in the CTD code.ACS chemical biology · 2012Article
- Article
- Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase.Biochimica et biophysica acta · 2010Article
- Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.BMC structural biology · 2009Article
- Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains.Journal of molecular biology · 2009Article
- Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research.Perspectives in medicinal chemistry · 2008Article
- Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.BMC genomics · 2006Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
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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