1PRT	Toxin	date	Nov 22, 1993
title	The Crystal Structure Of Pertussis Toxin
authors	P.E.Stein, R.J.Read
compound		source
Molecule: Pertussis Toxin (Subunit S1) Chain: A, G Engineered: Yes		Organism_scientific: Bordetella Pertussis
Molecule: Pertussis Toxin (Subunit S2) Chain: B, H Engineered: Yes		Organism_scientific: Bordetella Pertussis
Molecule: Pertussis Toxin (Subunit S3) Chain: C, I Engineered: Yes		Organism_scientific: Bordetella Pertussis
Molecule: Pertussis Toxin (Subunit S4) Chain: D, E, J, K Engineered: Yes		Organism_scientific: Bordetella Pertussis
Molecule: Pertussis Toxin (Subunit S5) Chain: F, L Engineered: Yes		Organism_scientific: Bordetella Pertussis
symmetry	Space Group: P 21 21 21	R_factor	0.195
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	2.90 Å
note	1PRT (Molecule of the Month:pdb69)
related structures	by homologous chain: 1BCP
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	The crystal structure of pertussis toxin., Stein PE, Boodhoo A, Armstrong GD, Cockle SA, Klein MH, Read RJ, Structure 1994 Jan 15;2(1):45-57. PMID:8075982

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (297 Kb) [Save to disk] Biological Unit Coordinates (1prt.pdb1.gz) 148 Kb Biological Unit Coordinates (1prt.pdb2.gz) 150 Kb CSU: Contacts of Structural Units for 1PRT Likely Quarternary Molecular Structure file(s) for 1PRT Retrieve 1PRT in mmCIF format [Save to disk]

View 1PRT in 3D

Proteopedia, because life has more than 2D. On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1PRT

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1PRT, from MSDmotif at EBI Genome occurence of 1PRT's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1prta_, region A [Jmol] [rasmolscript] [script source]     - Domain d1prtb2, region B:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1prtb1, region B:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1prtc2, region C:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1prtc1, region C:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1prtd_, region D [Jmol] [rasmolscript] [script source]     - Domain d1prte_, region E [Jmol] [rasmolscript] [script source]     - Domain d1prtf_, region F [Jmol] [rasmolscript] [script source]     - Domain d1prtg_, region G [Jmol] [rasmolscript] [script source]     - Domain d1prth2, region H:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1prth1, region H:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1prti2, region I:4-89 [Jmol] [rasmolscript] [script source]     - Domain d1prti1, region I:90-199 [Jmol] [rasmolscript] [script source]     - Domain d1prtj_, region J [Jmol] [rasmolscript] [script source]     - Domain d1prtk_, region K [Jmol] [rasmolscript] [script source]     - Domain d1prtl_, region L [Jmol] [rasmolscript] [script source] Fold representative 1prt 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: [1prt_K] [1prt_G] [1prt_E] [1prt_F] [1prt_B] [1prt_L] [1prt_D] [1prt_I] [1prt_H] [1prt_C] [1prt_A] [1prt_J]

Other resources with information on 1PRT

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

Movements, Movies and Images

Domain movements in 1PRT from the Database of Macromolecular Movements. Images from IMB Jena Image Library of Biological Macromolecules.

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