8SM5: BHRF1 from Epstein Barr Virus

Crystal Structure of BHRF1 from Epstein Barr Virus in complex with BID BH3 peptide. Determined by X-ray diffraction at 2.61 Å resolution. Released 11 Oct 2023.

Method: X-ray diffraction
Resolution: 2.61 Å
Organisms: Human herpesvirus 4 strain B95-8, Homo sapiens
Chains: 10
Atoms: 6,850
Mol. weight: 99.73 kDa
Released: 11 Oct 2023

Explore 8SM5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SM5 contains 57 α-helices and 0 β-strands across 10 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	27-35	9
α-helix	45-60	16
α-helix	62-75	14
α-helix	79-91	13
α-helix	98-116	19
α-helix	123-137	15
α-helix	138-140	3
α-helix	141-147	7
α-helix	150-155	6

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	82-96	15

Chain C: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	27-35	9
α-helix	45-60	16
α-helix	62-75	14
α-helix	79-91	13
α-helix	98-116	19
α-helix	123-137	15
α-helix	138-140	3
α-helix	141-146	6
α-helix	150-155	6

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	83-95	13

Chain E: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	27-35	9
α-helix	45-60	16
α-helix	62-75	14
α-helix	79-87	9
α-helix	88-92	5
α-helix	98-116	19
α-helix	123-137	15
α-helix	138-140	3
α-helix	141-146	6
α-helix	150-156	7

Chains F and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	82-95	14

Chain G: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	27-35	9
α-helix	45-60	16
α-helix	62-73	12
α-helix	79-91	13
α-helix	98-116	19
α-helix	123-136	14
α-helix	137-140	4
α-helix	141-146	6
α-helix	150-155	6

Chain I: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	5-18	14
α-helix	27-35	9
α-helix	45-60	16
α-helix	62-75	14
α-helix	79-86	8
α-helix	106-116	11
α-helix	123-136	14
α-helix	137-140	4
α-helix	141-146	6
α-helix	150-155	6

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator BHRF1	A, C, E, G, I	protein	156	Human herpesvirus 4 strain B95-8	P03182 (AlphaFold model)
Bid BH3	B, D, F, H, J	protein	18	Homo sapiens	P55957 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I), FASTA

>8SM5_1 Apoptosis regulator BHRF1 (chains A, C, E, G, I)
AYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVVLRYHVLLEEIIERN
SETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAWCMHACRTLCCNQST
PYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDN

Sequence of entity 2 (B, D, F, H, J), FASTA

>8SM5_2 BID BH3 (chains B, D, F, H, J)
DIIRNIARHLAQVGDSMD

Primary citation

Epstein-Barr Virus Encoded BCL2, BHRF1, Downregulates Autophagy by Noncanonical Binding of BECN1. Wyatt, S., Glover, K., Dasanna, S. et al. Biochemistry (2023) 62:2934-2951. DOI 10.1021/acs.biochem.3c00225 · PubMed

Other PDB entries of the same protein (UniProt P03182 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7P9W 2.0 Å, Epstein-Barr virus encoded apoptosis regulator BHRF1 in complex with Puma BH3
2XPX 2.05 Å, Crystal structure of BHRF1:Bak BH3 complex
7P33 2.79 Å, Epstein-Barr virus encoded Bcl-2 homolog BHRF-1 in complex with Bid BH3 peptide
1Q59 Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2

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