1BCP	Toxin	date	Nov 21, 1995
title	Binary Complex Of Pertussis Toxin And Atp
authors	B.Hazes, R.J.Read
compound		source
Molecule: Pertussis Toxin Chain: A, G Ec: 2.4.2.-		Organism_scientific: Bordetella Pertussis Strain: 10536 Other_details: The Pertussis Toxin Used For This Work Was Purified From B. Pertussis Strain 10536 (Loosmore Et Al., Nucleic Acids Res., Vol. 17, 8365, 1989), Which Differs At Two Positions In Subunit S1 (Asp 34 Glu And Ile 198 Val) From The Sequence That Was First Reported For The Protein (Nicosia Et Al., Pnas Vol 83, 4631 - 4635, 1986).;
Molecule: Pertussis Toxin Chain: B, H Ec: 2.4.2.-		Organism_scientific: Bordetella Pertussis Strain: 10536 Other_details: The Pertussis Toxin Used For This Work Was Purified From B. Pertussis Strain 10536 (Loosmore Et Al., Nucleic Acids Res., Vol. 17, 8365, 1989), Which Differs At Two Positions In Subunit S1 (Asp 34 Glu And Ile 198 Val) From The Sequence That Was First Reported For The Protein (Nicosia Et Al., Pnas Vol 83, 4631 - 4635, 1986).;
Molecule: Pertussis Toxin Chain: C, I Ec: 2.4.2.-		Organism_scientific: Bordetella Pertussis Strain: 10536 Other_details: The Pertussis Toxin Used For This Work Was Purified From B. Pertussis Strain 10536 (Loosmore Et Al., Nucleic Acids Res., Vol. 17, 8365, 1989), Which Differs At Two Positions In Subunit S1 (Asp 34 Glu And Ile 198 Val) From The Sequence That Was First Reported For The Protein (Nicosia Et Al., Pnas Vol 83, 4631 - 4635, 1986).;
Molecule: Pertussis Toxin Chain: D, E, J, K Ec: 2.4.2.-		Organism_scientific: Bordetella Pertussis Strain: 10536 Other_details: The Pertussis Toxin Used For This Work Was Purified From B. Pertussis Strain 10536 (Loosmore Et Al., Nucleic Acids Res., Vol. 17, 8365, 1989), Which Differs At Two Positions In Subunit S1 (Asp 34 Glu And Ile 198 Val) From The Sequence That Was First Reported For The Protein (Nicosia Et Al., Pnas Vol 83, 4631 - 4635, 1986).;
Molecule: Pertussis Toxin Chain: F, L Ec: 2.4.2.-		Organism_scientific: Bordetella Pertussis Strain: 10536 Other_details: The Pertussis Toxin Used For This Work Was Purified From B. Pertussis Strain 10536 (Loosmore Et Al., Nucleic Acids Res., Vol. 17, 8365, 1989), Which Differs At Two Positions In Subunit S1 (Asp 34 Glu And Ile 198 Val) From The Sequence That Was First Reported For The Protein (Nicosia Et Al., Pnas Vol 83, 4631 - 4635, 1986).
symmetry	Space Group: P 21 21 21	R_factor	0.232
crystal cell	length a length b length c angle alpha angle beta angle gamma 163.800 98.200 194.500 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.70 Å
ligand	ATP	enzyme	Transferase E.C.2.4.2 BRENDA
note	1BCP is a representative structure
related structures	by homologous chain: 1PRT
domain	The region which spans amino-acids 42-49 is required for enzymatic activity and contributes to the formation of a potentially important antigenic determinant.
similarity	Belongs to the pertussis toxin s2/s3 subunits family.[Pertussis_S1]
subunit	Pertussis toxin contains five different chains, s1-s5. They are organized into 2 functional subunits: a, composed of s1 (which is toxic) and b, containing s2, s3, s5, and two copies of s4 (b binds to the membrane receptors). Dimers of s2-s4 and s3-s4 are held together by s5.
Genes	BP3783, BP3784, BP3785, BP3786, BP3787, PTXA, PTXB, PTXC, PTXD, PTXE (B. pertussis)
function	In the absence of g proteins it also catalyzes the cleavage of nad(+) into adp-ribose and nicotinamide. Ptx oligomer b binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. It catalyzes the adp-ribosylation of a cysteine in the alpha subunit of heterotrimeric g proteins. It irreversibly uncouples the g-alpha gtp-binding proteins from their membrane receptors. S1 is an nad-dependent adp-ribosyltransferase.
Gene Ontology	Chain Function Process Component A, G NAD+ ADP-ribosyltransferase ... transferase activity transferase activity, transf... pathogenesis extracellular region B, H, C, I pathogenesis extracellular region membrane F, J, K, E, D, L pathogenesis membrane
Primary reference	Crystal structure of the pertussis toxin-ATP complex: a molecular sensor., Hazes B, Boodhoo A, Cockle SA, Read RJ, J Mol Biol 1996 May 17;258(4):661-71. PMID:8637000

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (299 Kb) [Save to disk] Biological Unit Coordinates (1bcp.pdb1.gz) 151 Kb Biological Unit Coordinates (1bcp.pdb2.gz) 149 Kb CSU: Contacts of Structural Units for 1BCP Likely Quarternary Molecular Structure file(s) for 1BCP Structure Factors (635 Kb) Retrieve 1BCP in mmCIF format [Save to disk]

View 1BCP in 3D

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Visual 3D analysis of 1BCP

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Structure-derived information

Electron Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1BCP, from MSDmotif at EBI Genome occurence of 1BCP's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1bcpa_, region A [Jmol] [rasmolscript] [script source]     - Domain d1bcpb2, region B:3-89 [Jmol] [rasmolscript] [script source]     - Domain d1bcpb1, region B:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1bcpc2, region C:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1bcpc1, region C:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1bcpd_, region D [Jmol] [rasmolscript] [script source]     - Domain d1bcpe_, region E [Jmol] [rasmolscript] [script source]     - Domain d1bcpf_, region F [Jmol] [rasmolscript] [script source]     - Domain d1bcpg_, region G [Jmol] [rasmolscript] [script source]     - Domain d1bcph2, region H:3-89 [Jmol] [rasmolscript] [script source]     - Domain d1bcph1, region H:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1bcpi2, region I:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1bcpi1, region I:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1bcpj_, region J [Jmol] [rasmolscript] [script source]     - Domain d1bcpk_, region K [Jmol] [rasmolscript] [script source]     - Domain d1bcpl_, region L [Jmol] [rasmolscript] [script source] Fold representative 1bcp from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1bcp_K] [1bcp_B] [1bcp_L] [1bcp_C] [1bcp_D] [1bcp_F] [1bcp_J] [1bcp_H] [1bcp_G] [1bcp_A] [1bcp_E] [1bcp_I]

Other resources with information on 1BCP

InterPro: IPR005138 , IPR003899 , IPR003898 PDBREPORT (protein verification by WHAT_CHECK procedures) MMDB (Entrez's Structure Database)

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