3VU7: REV1-REV7-REV3 ternary complex

Crystal structure of REV1-REV7-REV3 ternary complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 8 Aug 2012.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,516
Mol. weight: 45.83 kDa
Released: 8 Aug 2012

Explore 3VU7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VU7 contains 15 α-helices and 10 β-strands across 3 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 C: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	12-33	22
α-helix	39-41	3
β-strand	42-47	6	2
β-strand	50-55	6	2
α-helix	58-76	19
β-strand	80-88	9	1
β-strand	94-103	10	1
α-helix	115-131	17
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-152	8	1
α-helix	157-163	7
β-strand	171-173	3	1
α-helix	174-175	2
α-helix	176-179	4
β-strand	184-192	9	1
β-strand	198-206	9	1

Chain H: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	1165-1179	15
α-helix	1184-1199	16
α-helix	1203-1218	16
α-helix	1224-1243	20
β-strand	1247	1	1

Chain Z: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1877-1880	4	1
α-helix	1883-1886	4
α-helix	1887-1891	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein REV1	H	protein	124	Homo sapiens	Q9UBZ9 (AlphaFold model)
Mitotic spindle assembly checkpoint protein MAD2B	C	protein	227	Homo sapiens	Q9UI95 (AlphaFold model)
DNA polymerase zeta catalytic subunit	Z	protein	52	Homo sapiens	O60673

Sequence of entity 1 (H), FASTA

>3VU7_1 DNA repair protein REV1 (chains H)
MRGSHHHHHHGSGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDI
LQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGST
LKVT

Sequence of entity 2 (C), FASTA

>3VU7_2 Mitotic spindle assembly checkpoint protein MAD2B (chains C)
MGSSHHHHHHSQDPNSMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQK
RKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQ
PPLLSISSDSLLSHVEQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQ
VIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS

Sequence of entity 3 (Z), FASTA

>3VU7_3 DNA polymerase zeta catalytic subunit (chains Z)
MLTPTPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHD

Primary citation

Structural basis of recruitment of DNA polymerase [zeta] by interaction between REV1 and REV7 proteins. Kikuchi, S., Hara, K., Shimizu, T. et al. J Biol Chem (2012) 287:33847-33852. DOI 10.1074/jbc.M112.396838 · PubMed

Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4EXT 1.9 Å, Structure of polymerase-interacting domain of human Rev1 in complex with translesional…
6WS0 2.24 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
6ASR 2.36 Å, REV1 UBM2 domain complex with ubiquitin
6WS5 2.47 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
3GQC 2.5 Å, Structure of human Rev1-DNA-dNTP ternary complex
4GK0 2.7 Å, Crystal structure of human Rev3-Rev7-Rev1 complex
9VGW 2.7 Å, Crystal structure of human PCNA in complex with REV1 PIP-box
4BA9 2.73 Å, The structural basis for the coordination of Y-family Translesion DNA Polymerases by Rev1
4GK5 3.21 Å, Crystal structure of human Rev3-Rev7-Rev1-Polkappa complex
2EBW Solution structure of the BRCT domain from human DNA repair protein REV1
2LSI Solution structure of polymerase-interacting domain of human Rev1 in complex with…
2LSK C-terminal domain of human REV1 in complex with DNA-polymerase H (eta)

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