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PDBsum entry 1yw5

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protein links
Isomerase PDB id
1yw5
Jmol
Contents
Protein chain
177 a.a. *
Waters ×369
* Residue conservation analysis
PDB id:
1yw5
Name: Isomerase
Title: Peptidyl-prolyl isomerase ess1 from candida albicans
Structure: Peptidyl prolyl cis/trans isomerase. Chain: a. Engineered: yes
Source: Candida albicans. Organism_taxid: 5476. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.200     R-free:   0.242
Authors: Z.Li,H.Li,G.Devasahayam,T.Gemmill,V.Chaturvedi,S.D.Hanes, P.Van Roey
Key ref:
Z.Li et al. (2005). The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility. Biochemistry, 44, 6180-6189. PubMed id: 15835905 DOI: 10.1021/bi050115l
Date:
17-Feb-05     Release date:   26-Apr-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q59KZ2  (Q59KZ2_CANAL) -  Uncharacterized protein
Seq:
Struc:
177 a.a.
177 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   9 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
DOI no: 10.1021/bi050115l Biochemistry 44:6180-6189 (2005)
PubMed id: 15835905  
 
 
The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.
Z.Li, H.Li, G.Devasahayam, T.Gemmill, V.Chaturvedi, S.D.Hanes, P.Van Roey.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19309529 O.Heikkinen, R.Seppala, H.Tossavainen, S.Heikkinen, H.Koskela, P.Permi, and I.Kilpeläinen (2009).
Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.
  BMC Struct Biol, 9, 17.
PDB code: 2jzv
19038264 T.A.Cutler, B.M.Mills, D.J.Lubin, L.T.Chong, and S.N.Loh (2009).
Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains.
  J Mol Biol, 386, 854-868.  
  19787094 J.W.Mueller, and P.Bayer (2008).
Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research.
  Perspect Medicin Chem, 2, 11-20.  
16995943 T.J.Pemberton (2006).
Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.
  BMC Genomics, 7, 244.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.