6AW2: HopQ-CEACAM1 complex

Crystal structure of the HopQ-CEACAM1 complex. Determined by X-ray diffraction at 2.68 Å resolution. Released 16 May 2018.

Method: X-ray diffraction
Resolution: 2.68 Å
Organisms: Homo sapiens, Helicobacter pylori
Chains: 2
Atoms: 3,435
Mol. weight: 59.13 kDa
Released: 16 May 2018

Explore 6AW2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6AW2 contains 16 α-helices and 27 β-strands across 2 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: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	10-11	2	2
β-strand	17-22	6	1
β-strand	28-35	8	3
α-helix	41-43	3
β-strand	44-49	6	3
β-strand	55-57	3	3
β-strand	65-67	3	1
β-strand	73-75	3	1
α-helix	80-82	3
β-strand	84-92	9	3
β-strand	96	1	4
β-strand	97-104	8	3
β-strand	105-106	2	2

Chain B: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	53-72	20
α-helix	78-97	20
α-helix	98-100	3
β-strand	101	1	5
β-strand	103	1	6
β-strand	106	1	7
β-strand	116-120	5	8
β-strand	128-132	5	8
β-strand	135-136	2	4
β-strand	142-143	2	4
α-helix	147-149	3
β-strand	151	1	7
β-strand	158	1	6
α-helix	160-179	20
α-helix	182-184	3
β-strand	191-201	11	8
β-strand	207-217	11	8
α-helix	220-237	18
α-helix	239	1
β-strand	240	1	9
β-strand	241	1	5
α-helix	242-243	2
β-strand	268	1	9
α-helix	269-298	30
α-helix	301-305	5
α-helix	318-350	33
β-strand	372-374	3	8
α-helix	388-404	17
α-helix	406-417	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carcinoembryonic antigen-related cell adhesion molecule 1	A	protein	109	Homo sapiens	P13688 (AlphaFold model)
HopQ	B	protein	439	Helicobacter pylori	H6A3H4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6AW2_1 Carcinoembryonic antigen-related cell adhesion molecule 1 (chains A)
MAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPG
PANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVY

Sequence of entity 2 (B), FASTA

>6AW2_2 HopQ (chains B)
MGSSHHHHHHSQDPVQKVKNADKVQKLSDTYEQLSRLLTNDNGTNSKTSAQAINQAVNNL
NERAKTLAGGTTNSPAYQATLLALRSVLGLWNSMGYAVICGGYTKSPGENNQKNFHYTDE
NGNGTTINCGGSTNSNGTHSSNGTNTLKADKNVSLSIEQYEKIHESYQILSKALKQAGLA
PLNSKGEKLEAHVTTSKYQQDSQTKTTTSVIDTTNDAQNLLTQAQTIVNTLKDYCPMLIA
KSSSGSGGGAATNTPSWQTAGGGKNSCETFGAEFSAASDMINNAQKIVQETQQLSANQPK
NITQPHNLNLNTPSSLTALAQKMLKNAQSQAEILKLANQVESDFNKLSSGHLKDYIGKCD
MSAISSTNMTMQSQKNNWGNGCAGVEETLTSLKTSAADFNNQTPQINQAQNLANTLIQEL
GNNPFRNMGMIASSTTNNG

Primary citation

TheHelicobacter pyloriadhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA. Bonsor, D.A., Zhao, Q., Schmidinger, B. et al. EMBO J (2018) 37. DOI 10.15252/embj.201798664 · PubMed

Other PDB entries of the same protein (UniProt P13688 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7MU8 1.7 Å, Structure of the minimally glycosylated human CEACAM1 N-terminal domain
6XO1 1.76 Å, Crystal structure of N97A mutant of human CEACAM1
23VF 1.79 Å, Crystal structure of CEACAM1 in complex with MG1124 antibody
6XNO 1.9 Å, Crystal structure of E99A mutant of human CEACAM1
6XNW 1.9 Å, Crystal structure of V39A mutant of human CEACAM1
4QXW 2.04 Å, Crystal structure of the human CEACAM1 membrane distal amino terminal (N)-domain
9U94 2.11 Å, Cryo-EM structure of Fusobacterium nucleatum CbpF in complex with human CEACAM1
2GK2 2.2 Å, Crystal structure of the N terminal domain of human CEACAM1
7RPP 2.2 Å, Crystal structure of human CEACAM1 with GFCC' and ABED face
4WHD 2.5 Å, Human CEACAM1 N-domain homodimer
6GBH 2.59 Å, Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
9GH5 2.7 Å, Complex of Fusobacterium nucleatum CbpF with human CEACAM1

Browse structure collections

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