4IRV: Helicobacter pylori CagA Oncogene

Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2. Determined by X-ray diffraction at 2.04 Å resolution. Released 15 Jan 2014.

Method: X-ray diffraction
Resolution: 2.04 Å
Organisms: Helicobacter pylori, Homo sapiens
Chains: 8
Atoms: 7,530
Mol. weight: 128.36 kDa
Released: 15 Jan 2014

Explore 4IRV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IRV contains 59 α-helices and 0 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	25-44	20
α-helix	46-48	3
α-helix	49-79	31
α-helix	81-83	3
α-helix	84-101	18
α-helix	107-117	11
α-helix	119-130	12
α-helix	135-137	3
α-helix	140-145	6
α-helix	146-150	5
α-helix	158-182	25
α-helix	185-190	6
α-helix	192-201	10
α-helix	212-217	6

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	25-44	20
α-helix	46-48	3
α-helix	49-79	31
α-helix	81-83	3
α-helix	84-101	18
α-helix	107-117	11
α-helix	119-130	12
α-helix	135-137	3
α-helix	140-149	10
α-helix	158-182	25
α-helix	185-190	6
α-helix	192-201	10
α-helix	212-217	6

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	25-44	20
α-helix	46-48	3
α-helix	49-79	31
α-helix	81-83	3
α-helix	84-101	18
α-helix	107-117	11
α-helix	119-130	12
α-helix	135-137	3
α-helix	140-145	6
α-helix	146-150	5
α-helix	158-182	25
α-helix	185-190	6
α-helix	192-200	9
α-helix	212-217	6

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	24-44	21
α-helix	46-48	3
α-helix	49-79	31
α-helix	81-83	3
α-helix	84-102	19
α-helix	107-117	11
α-helix	119-131	13
α-helix	135-137	3
α-helix	140-145	6
α-helix	146-150	5
α-helix	158-182	25
α-helix	185-190	6
α-helix	192-201	10
α-helix	212-217	6

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	747-760	14

Chains F, G and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	747-761	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytotoxicity-associated immunodominant antigen	A, B, C, D	protein	221	Helicobacter pylori	P55980 (AlphaFold model)
Apoptosis-stimulating of p53 protein 2	E, F, G, H	protein	62	Homo sapiens	Q13625 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4IRV_1 Cytotoxicity-associated immunodominant antigen (chains A, B, C, D)
GPVDTAFDPQQFINNLQVAFIKVDNVVASFDPDQKPIVDKNDRDNRQAFDGISQLREEYS
NKAIKNPTKKNQYFSDFIDKSNDLINKDNLIDVESSTKSFQKFGDQRYQIFTSWVSHQKD
PSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDES
LKERQEAEKNGGPTGGDWLDIFLSFIFNKKQSSDVKEAINQ

Sequence of entity 2 (E, F, G, H), FASTA

>4IRV_2 Apoptosis-stimulating of p53 protein 2 (chains E, F, G, H)
GPKLASNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTAS
SE

Primary citation

Structure of the Helicobacter pylori CagA oncoprotein bound to the human tumor suppressor ASPP2. Nesic, D., Buti, L., Lu, X. et al. Proc Natl Acad Sci U S A (2014) 111:1562-1567. DOI 10.1073/pnas.1320631111 · PubMed

Other PDB entries of the same protein (UniProt P55980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3IEC 2.2 Å, Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
5X7B 2.45 Å, Crystal structure of SHP2_SH2-CagA EPIYA_C peptide complex
5X94 2.6 Å, Crystal structure of SHP2_SH2-CagA EPIYA_D peptide complex
4DVZ 3.19 Å, Crystal structure of the Helicobacter pylori CagA oncoprotein
4DVY 3.3 Å, Crystal structure of the Helicobacter pylori CagA oncoprotein
4G0H 3.6 Å, Crystal structure of the N-terminal domain of Helicobacter pylori CagA protein

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