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PDBsum entry 1x9y

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protein Protein-protein interface(s) links
Hydrolase PDB id
1x9y
Jmol
Contents
Protein chains
346 a.a.
Waters ×243
PDB id:
1x9y
Name: Hydrolase
Title: The prostaphopain b structure
Structure: Cysteine proteinase. Chain: a, b, c, d. Fragment: proenzyme (residues 37-393). Engineered: yes
Source: Staphylococcus aureus. Organism_taxid: 1280. Gene: sspb. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.50Å     R-factor:   0.244     R-free:   0.276
Authors: R.Filipek,R.Szczepanowski,A.Sabat,J.Potempa,M.Bochtler
Key ref:
R.Filipek et al. (2004). Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition. Biochemistry, 43, 14306-14315. PubMed id: 15518582 DOI: 10.1021/bi048661m
Date:
24-Aug-04     Release date:   23-Nov-04    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0C1S6  (SSPB_STAAU) -  Staphopain B
Seq:
Struc:
393 a.a.
346 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     pathogenesis   2 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
DOI no: 10.1021/bi048661m Biochemistry 43:14306-14315 (2004)
PubMed id: 15518582  
 
 
Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition.
R.Filipek, R.Szczepanowski, A.Sabat, J.Potempa, M.Bochtler.
 
  ABSTRACT  
 
Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central half-barrel or barrel-sandwich hybrid and occludes primed, but not nonprimed, sites in the active site cleft of the protease. The structure of the mature part of the protease is similar to previously reported staphopain structures, and no distortion of the catalytic residues is apparent at 2.5 A resolution. A comparison of prostaphopain B with the staphopain B-staphostatin B complex shows that the proregion and the inhibitor interact with largely nonoverlapping parts of the protease surface. In a modeled complex of prostaphopain B with staphostatin B, clashes occur both inside and outside the active site cleft, but involve mostly poorly ordered regions of the protein that may be mobile.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19943908 N.Nickerson, J.Ip, D.T.Passos, and M.J.McGavin (2010).
Comparison of Staphopain A (ScpA) and B (SspB) precursor activation mechanisms reveals unique secretion kinetics of proSspB (Staphopain B), and a different interaction with its cognate Staphostatin, SspC.
  Mol Microbiol, 75, 161-177.  
18205806 A.M.Calander, G.Dubin, J.Potempa, and A.Tarkowski (2008).
Staphylococcus aureus infection triggers production of neutralizing, V8 protease-specific antibodies.
  FEMS Immunol Med Microbiol, 52, 267-272.  
18026858 B.Władyka, and K.Pustelny (2008).
Regulation of bacterial protease activity.
  Cell Mol Biol Lett, 13, 212-229.  
17993455 N.Mallorquí-Fernández, S.P.Manandhar, G.Mallorquí-Fernández, I.Usón, K.Wawrzonek, T.Kantyka, M.Solà, I.B.Thøgersen, J.J.Enghild, J.Potempa, and F.X.Gomis-Rüth (2008).
A New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain A.
  J Biol Chem, 283, 2871-2882.
PDB codes: 3bb7 3bba
16339904 D.Vivares, P.Arnoux, and D.Pignol (2005).
A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.
  Proc Natl Acad Sci U S A, 102, 18848-18853.
PDB codes: 2btw 2bu3
16045606 J.Potempa, E.Golonka, R.Filipek, and L.N.Shaw (2005).
Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases.
  Mol Microbiol, 57, 605-610.  
15716447 L.N.Shaw, E.Golonka, G.Szmyd, S.J.Foster, J.Travis, and J.Potempa (2005).
Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype.
  J Bacteriol, 187, 1751-1762.  
16333395 M.A.Meehl, J.S.Pinkner, P.J.Anderson, S.J.Hultgren, and M.G.Caparon (2005).
A novel endogenous inhibitor of the secreted streptococcal NAD-glycohydrolase.
  PLoS Pathog, 1, e35.  
16045611 T.F.Kagawa, P.W.O'toole, and J.C.Cooney (2005).
SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes.
  Mol Microbiol, 57, 650-666.  
15897280 T.Imamura, S.Tanase, G.Szmyd, A.Kozik, J.Travis, and J.Potempa (2005).
Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus.
  J Exp Med, 201, 1669-1676.  
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 codes are shown on the right.