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PDBsum entry 1due

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Toxin, hydrolase PDB id
1due
Jmol
Contents
Protein chain
242 a.a. *
Waters ×41
* Residue conservation analysis
PDB id:
1due
Name: Toxin, hydrolase
Title: Crystal structure of exfoliative toxin a s195a mutant
Structure: Exfoliative toxin a. Chain: a. Engineered: yes. Mutation: yes
Source: Staphylococcus aureus. Organism_taxid: 1280. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: chromosomal DNA of s. Aureus isolated from a patient with staphylococcal scalded skin disease
Resolution:
2.00Å     R-factor:   0.214     R-free:   0.238
Authors: A.C.Papageorgiou,L.R.W.Plano,C.M.Collins,K.R.Acharya
Key ref: A.C.Papageorgiou et al. (2000). Structural similarities and differences in Staphylococcus aureus exfoliative toxins A and B as revealed by their crystal structures. Protein Sci, 9, 610-618. PubMed id: 10752623 DOI: 10.1110/ps.9.3.610
Date:
17-Jan-00     Release date:   21-Jan-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09331  (ETA_STAAU) -  Exfoliative toxin A
Seq:
Struc:
280 a.a.
242 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     5 terms  

 

 
DOI no: 10.1110/ps.9.3.610 Protein Sci 9:610-618 (2000)
PubMed id: 10752623  
 
 
Structural similarities and differences in Staphylococcus aureus exfoliative toxins A and B as revealed by their crystal structures.
A.C.Papageorgiou, L.R.Plano, C.M.Collins, K.R.Acharya.
 
  ABSTRACT  
 
Staphylococcal aureus epidermolytic toxins (ETs) A and B are responsible for the induction of staphylococcal scalded skin syndrome, a disease of neonates and young children. The clinical features of this syndrome vary from localized blisters to severe exfoliation affecting most of the body surface. Comparison of the crystal structures of two subtypes of ETs-rETA (at 2.0 A resolution), rETB (at 2.8 A resolution), and an active site variant of rETA, Ser195Ala at 2.0 A resolution has demonstrated that their overall topology resembles that of a "trypsin-like" serine protease, but with significant differences at the N- and C-termini and loop regions. The details of the catalytic site in both ET structures are very similar to those in glutamate-specific serine proteases, suggesting a common catalytic mechanism. However, the "oxyanion hole," which is part of the catalytic sites of glutamate specific serine proteases, is in the closed or inactive conformation for rETA, yet in the open or active conformation for rETB. The ETs contain a unique amphipathic helix at the N-terminus, and it appears to be involved in optimizing the conformation of the catalytic site residues. Determination of the structure of the rETA catalytic site variant, Ser195Ala, showed no significant perturbation at the active site, establishing that the loss of biological and esterolytic activity can be attributed solely to disruption of the catalytic serine residue. Finally, the crystal structure of ETs, together with biochemical data and mutagenesis studies, strongly confirms the classification of these molecules as "serine proteases" rather than "superantigens."
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20875053 K.Iyori, J.Hisatsune, T.Kawakami, S.Shibata, N.Murayama, K.Ide, M.Nagata, T.Fukata, T.Iwasaki, K.Oshima, M.Hattori, M.Sugai, and K.Nishifuji (2010).
Identification of a novel Staphylococcus pseudintermedius exfoliative toxin gene and its prevalence in isolates from canines with pyoderma and healthy dogs.
  FEMS Microbiol Lett, 312, 169-175.  
17397555 L.Daugaard, L.O.Andresen, and M.Fredholm (2007).
Investigation of SNPs in the porcine desmoglein 1 gene.
  BMC Vet Res, 3, 4.  
17075192 M.Amagai (2006).
[Desmoglein, the target molecule in autoimmunity and infection]
  Nihon Rinsho Meneki Gakkai Kaishi, 29, 325-333.  
12880431 Y.Hanakawa, T.Selwood, D.Woo, C.Lin, N.M.Schechter, and J.R.Stanley (2003).
Calcium-dependent conformation of desmoglein 1 is required for its cleavage by exfoliative toxin.
  J Invest Dermatol, 121, 383-389.  
  12093888 Y.Hanakawa, N.M.Schechter, C.Lin, L.Garza, H.Li, T.Yamaguchi, Y.Fudaba, K.Nishifuji, M.Sugai, M.Amagai, and J.R.Stanley (2002).
Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome.
  J Clin Invest, 110, 53-60.  
11442563 S.Ladhani (2001).
Recent developments in staphylococcal scalded skin syndrome.
  Clin Microbiol Infect, 7, 301-307.  
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.