Annotation for this protein is in progress - please check future releases for more complete information


DP00280: Perfringolysin OFASTA viewXML view

General information
DisProt:DP00280
Name:Perfringolysin O
Synonym(s):TACY_CLOPE
Theta-toxin
Thiol-activated cytolysin
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P0C2E9
UniGene: 
SwissProt: TACY_CLOPE
TrEMBL:  
NCBI (GI): 124053391
Source organism:Clostridium perfringens
Sequence length:500
Percent disordered:10%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MIRFKKTKLI ASIAMALCLF SQPVISFSKD ITDKNQSIDS GISSLSYNRN EVLASNGDKI - 60
ESFVPKEGKK TGNKFIVVER QKRSLTTSPV DISIIDSVND RTYPGALQLA DKAFVENRPT - 120
ILMVKRKPIN INIDLPGLKG ENSIKVDDPT YGKVSGAIDE LVSKWNEKYS STHTLPARTQ - 180
YSESMVYSKS QISSALNVNA KVLENSLGVD FNAVANNEKK VMILAYKQIF YTVSADLPKN - 240
PSDLFDDSVT FNDLKQKGVS NEAPPLMVSN VAYGRTIYVK LETTSSSKDV QAAFKALIKN - 300
TDIKNSQQYK DIYENSSFTA VVLGGDAQEH NKVVTKDFDE IRKVIKDNAT FSTKNPAYPI - 360
SYTSVFLKDN SVAAVHNKTD YIETTSTEYS KGKINLDHSG AYVAQFEVAW DEVSYDKEGN - 420
EVLTHKTWDG NYQDKTAHYS TVIPLEANAR NIRIKARECT GLAWEWWRDV ISEYDVPLTN - 480
NINVSIWGTT LYPGSSITYN

Region 1: 190-217 Region 2: 288-311

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:TMH1
Location:190 - 217
Length:28
Region sequence:

SQISSALNVNAKVLENSLGVDFNAVANN

Modification type: Monomeric
Mutant
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Fluorescent probes (298 K; HEPES (pH 7.5) 50 mM; NaCl 100 mM)
References:
  1. Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM. "Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy." J Struct Biol. 2005; 150(1): 100-8. PubMed: 15797734

  2. Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK. "The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins." Cell. 1999; 99(3): 293-9. PubMed: 10555145
Comments:
The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate.


Region 2
Type:Disordered
Name:TMH2
Location:288 - 311
Length:24
Region sequence:

KDVQAAFKALIKNTDIKNSQQYKD

Modification type: Monomeric
Mutant
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Fluorescent probes (298 K; HEPES (pH 7.5) 50 mM; NaCl 100 mM)
References:
  1. Dang TX, Hotze EM, Rouiller I, Tweten RK, Wilson-Kubalek EM. "Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy." J Struct Biol. 2005; 150(1): 100-8. PubMed: 15797734

  2. Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK. "The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins." Cell. 1999; 99(3): 293-9. PubMed: 10555145
Comments:
The six alpha-helices in domain 3 undergo a conformational change into two beta-hairpins that span the membrane. This order to order transition proceeds through a disordered intermediate.


References

  1. Shepard LA, Heuck AP, Hamman BD, Rossjohn J, Parker MW, Ryan KR, Johnson AE, Tweten RK. "Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy." Biochemistry. 1998; 37(41): 14563-74. PubMed: 9772185


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