PDB ID or protein name

1ca1 » Alpha-toxin (PHLC1_CLOPE), open state

1ca1 » Alpha-toxin (PHLC1_CLOPE), open state
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Topology in Secreted
Topologyout side
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1ca1 » Alpha-toxin (PHLC1_CLOPE), open state
Depth 2.9 ± 1.0 Å
Tilt Angle 89 ± 4°
ΔGtransfer -9.3 kcal/mol
Links to 1ca1 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 1.9 Å
Other PDB entries representing this structure none
Number of subunits 1
Experimental Verification for 1ca1 » Alpha-toxin (PHLC1_CLOPE), open state
Results are consistent with the important role of Y331 and F334 for asociation with lipid bilayers (Jepson et al. 2001).
1 reference
Jepson M, Bullifent HL, Crane D, Flores-Diaz M, Alape-Giron A, Jayasekeera P, Lingard B, Moss D, Titball RW. 2001. Tyrosine 331 and phenylalanine 334 in Clostridium perfringens alpha-toxin are essential for cytotoxic activity. FEBS Lett. 495:172-7. PubMed
Comments on 1ca1 » Alpha-toxin (PHLC1_CLOPE), open state
Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca(2+) dependent manner and toxicity is conferred by this C-terminal domain, which also contributes to the sphingomyelinase activity.