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PDBsum entry 1j71
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Hydrolase PDB id
1j71

 

 

 

 

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Contents
Protein chain
334 a.a. *
Ligands
THR-ILE-THR-SER
EOH ×6
Waters ×231
* Residue conservation analysis
PDB id:
1j71
Name: Hydrolase
Title: Structure of the extracellular aspartic proteinase from candida tropicalis yeast.
Structure: Aspartic proteinase. Chain: a. Synonym: candidapepsin. Tetrapeptide thr-ile-thr-ser. Chain: b
Source: Candida tropicalis. Organism_taxid: 5482. Unidentified. Organism_taxid: 32644
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.165     R-free:   0.193
Authors: J.Symersky,M.Monod,S.I.Foundling
Key ref:
J.Symersky et al. (1997). High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast. Biochemistry, 36, 12700-12710. PubMed id: 9335526 DOI: 10.1021/bi970613x
Date:
15-May-01     Release date:   23-May-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q00663  (CARP_CANTR) -  Candidapepsin from Candida tropicalis
Seq:
Struc: 		394 a.a.
334 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.23.24  - candidapepsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.

 

 
DOI no: 10.1021/bi970613x Biochemistry 36:12700-12710 (1997)
PubMed id: 9335526  
 
 
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
J.Symersky, M.Monod, S.I.Foundling.
 
  ABSTRACT  
 
The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21411325 S.Silva, M.Negri, M.Henriques, R.Oliveira, D.W.Williams, and J.Azeredo (2011).
Adherence and biofilm formation of non-Candida albicans Candida species.
  Trends Microbiol, 19, 241-247.  
19166319 O.Hrusková-Heidingsfeldová, J.Dostál, F.Majer, J.Havlíkova, M.Hradilek, and I.Pichová (2009).
Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties.
  Biol Chem, 390, 259-268.  
16972793 F.Majer, L.Pavlícková, P.Majer, M.Hradilek, E.Dolejsí, O.Hrusková-Heidingsfeldová, and I.Pichová (2006).
Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling.
  Biol Chem, 387, 1247-1254.  
16673078 L.Coates, P.T.Erskine, S.Mall, R.Gill, S.P.Wood, D.A.Myles, and J.B.Cooper (2006).
X-ray, neutron and NMR studies of the catalytic mechanism of aspartic proteinases.
  Eur Biophys J, 35, 559-566.  
17042751 M.Merkerová, J.Dostál, M.Hradilek, I.Pichová, and O.Hrusková-Heidingsfeldová (2006).
Cloning and characterization of Sapp2p, the second aspartic proteinase isoenzyme from Candida parapsilosis.
  FEMS Yeast Res, 6, 1018-1026.  
16201875 J.Dostál, H.Dlouhá, P.Malon, I.Pichová, and O.Hrusková-Heidingsfeldová (2005).
The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase.
  Biol Chem, 386, 791-799.  
11119531 C.Zaugg, M.Borg-Von Zepelin, U.Reichard, D.Sanglard, and M.Monod (2001).
Secreted aspartic proteinase family of Candida tropicalis.
  Infect Immun, 69, 405-412.  
11322888 I.Pichová, L.Pavlícková, J.Dostál, E.Dolejsí, O.Hrusková-Heidingsfeldová, J.Weber, T.Ruml, and M.Soucek (2001).
Secreted aspartic proteases of Candida albicans, Candida tropicalis, Candida parapsilosis and Candida lusitaniae. Inhibition with peptidomimetic inhibitors.
  Eur J Biochem, 268, 2669-2677.  
11021803 L.Hong, G.Koelsch, X.Lin, S.Wu, S.Terzyan, A.K.Ghosh, X.C.Zhang, and J.Tang (2000).
Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.
  Science, 290, 150-153.
PDB code: 1fkn
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.

 

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