4FJO: Rev1 CTD-Rev3/7-Pol kappa RIR complex

Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex. Determined by X-ray diffraction at 2.72 Å resolution. Released 8 Aug 2012.

Method: X-ray diffraction
Resolution: 2.72 Å
Organism: Mus musculus
Chains: 4
Atoms: 2,995
Mol. weight: 40.9 kDa
Ligands: PO4
Released: 8 Aug 2012

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

Secondary structure: helices and β-sheets

4FJO contains 17 α-helices and 14 β-strands across 4 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: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	1157	1	1
β-strand	1160	1	1
α-helix	1163-1176	14
α-helix	1182-1197	16
α-helix	1201-1217	17
α-helix	1221-1242	22
β-strand	1245-1246	2	2

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	566-571	6

Chain C: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	3
α-helix	11-33	23
α-helix	39-41	3
β-strand	42-47	6	4
β-strand	50-55	6	4
α-helix	58-76	19
β-strand	80-88	9	2
β-strand	94-103	10	2
β-strand	109-111	3	3
α-helix	117-131	15
α-helix	133-136	4
α-helix	138-141	4
β-strand	145-152	8	2
α-helix	157-162	6
β-strand	171-173	3	2
α-helix	176-179	4
β-strand	184-192	9	2
β-strand	198-206	9	2

Chain D: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	1870-1873	4
β-strand	1874-1877	4	2
α-helix	1880-1883	4
α-helix	1884-1890	7
α-helix	1891-1893	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein REV1	A	protein	97	Mus musculus	Q920Q2 (AlphaFold model)
DNA polymerase kappa	B	protein	10	Mus musculus	Q9QUG2 (AlphaFold model)
Mitotic spindle assembly checkpoint protein MAD2B	C	protein	210	Mus musculus	Q9D752 (AlphaFold model)
DNA polymerase zeta catalytic subunit	D	protein	30	Mus musculus	Q61493

Sequence of entity 1 (A), FASTA

>4FJO_1 DNA repair protein REV1 (chains A)
AAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMK
RLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT

Sequence of entity 2 (B), FASTA

>4FJO_2 DNA polymerase kappa (chains B)
SFFDKKRSER

Sequence of entity 3 (C), FASTA

>4FJO_3 Mitotic spindle assembly checkpoint protein MAD2B (chains C)
MTTLTRQDLNFGQVVADVLSEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPEL
NQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSINSDSLLSHVE
QLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVH
MHDPRLIPLKTMTSDILKMQLYVEERAHKN

Sequence of entity 4 (D), FASTA

>4FJO_4 DNA polymerase zeta catalytic subunit (chains D)
GSFTPRTAHILKPLMSPPSREEIVATLLDH

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	8

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric Pol zeta and Pol kappa. Wojtaszek, J., Lee, C.J., D'Souza, S. et al. J Biol Chem (2012) 287:33836-33846. DOI 10.1074/jbc.M112.394841 · PubMed

Other PDB entries of the same protein (UniProt Q920Q2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6C8C 1.5 Å, Chimeric Pol kappa RIR Rev1 C-terminal domain in complex with JHRE06
6C59 2.03 Å, Chimeric Pol kappa RIR Rev1 C-terminal domain
2LSG Solution structure of the mouse Rev1 C-terminal domain
2LSJ Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region…

Browse structure collections

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