1UNN: DNA polymerase III beta subunit

Name: PDB 1UNN: Complex of beta-clamp processivity factor and little finger domain of PolIV
Published: 2003-11-06
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: beta-clamp

Complex of beta-clamp processivity factor and little finger domain of PolIV. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Nov 2003.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: ESCHERICHIA COLI
Chains: 4
Atoms: 8,485
Mol. weight: 108.57 kDa
Released: 6 Nov 2003

Explore 1UNN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UNN contains 37 α-helices and 69 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: 15 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
α-helix	7-17	11
α-helix	19-21	3
α-helix	28-31	4
β-strand	32-38	7	2
β-strand	41-47	7	2
β-strand	51-58	8	2
β-strand	64	1	1
β-strand	66-71	6	2
α-helix	72-81	10
α-helix	83	1
β-strand	87-92	6	1
β-strand	97-101	5	1
β-strand	104-108	5	1
β-strand	111	1	2
α-helix	117-118	2
β-strand	126-130	5	2
α-helix	132-140	9
α-helix	143-145	3
α-helix	153-155	3
β-strand	157-163	7	3
β-strand	166-172	7	3
β-strand	176-183	8	3
β-strand	191-196	6	3
α-helix	197-206	10
β-strand	214-218	5	2
β-strand	222-227	6	2
β-strand	230-235	6	2
α-helix	236	1
β-strand	237	1	3
α-helix	240-242	3
α-helix	244-247	4
β-strand	254-259	6	3
α-helix	260-272	13
β-strand	280-286	7	4
β-strand	289-295	7	4
β-strand	301-307	7	4
β-strand	309	1	3
β-strand	315-320	6	4
α-helix	321-331	11
β-strand	335-340	6	3
β-strand	347-351	5	3
β-strand	357-361	5	3
β-strand	364	1	4

Chain B: 16 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	4
α-helix	7-17	11
α-helix	28-31	4
β-strand	32-38	7	5
β-strand	41-47	7	5
β-strand	51-58	8	5
β-strand	63-64	2	4
β-strand	66-71	6	5
α-helix	72-81	10
α-helix	86	1
β-strand	87-93	7	4
β-strand	96-101	6	4
β-strand	104-109	6	4
β-strand	111	1	5
α-helix	113-115	3
α-helix	119-121	3
β-strand	124-131	8	5
α-helix	132-142	11
α-helix	143-145	3
α-helix	153-155	3
β-strand	157-172	16	6
β-strand	176-196	21	6
α-helix	197-206	10
β-strand	213-219	7	5
β-strand	222-227	6	5
β-strand	230-235	6	5
β-strand	237	1	6
α-helix	240-243	4
α-helix	244-247	4
β-strand	254-259	6	6
α-helix	260-272	13
β-strand	280-286	7	1
β-strand	289-295	7	1
β-strand	301-307	7	1
β-strand	309	1	6
β-strand	315-320	6	1
α-helix	321-331	11
β-strand	335-340	6	6
β-strand	347-351	5	6
β-strand	357-361	5	6
α-helix	362-363	2
β-strand	364	1	1
α-helix	365	1

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	242-253	12	7
α-helix	256-277	22
β-strand	282	1	8
β-strand	285-292	8	7
β-strand	297-303	7	7
β-strand	306	1	8
α-helix	309-323	15
β-strand	329-337	9	7
α-helix	338-343	6
β-strand	346	1	1

Chain D: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	242-253	12	9
α-helix	256-277	22
β-strand	285-292	8	9
β-strand	297-298	2	9
β-strand	301-303	3	9
α-helix	309-323	15
β-strand	329-337	9	9
α-helix	338-342	5
β-strand	346	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA polymerase III beta subunit	A, B	protein	366	ESCHERICHIA COLI	P0A988 (AlphaFold model)
DNA polymerase IV	C, D	protein	115	ESCHERICHIA COLI	Q47155 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1UNN_1 DNA POLYMERASE III BETA SUBUNIT (chains A, B)
MKFTVEREHLLKPLQQVSGPLGGRPTLPILGNLLLQVADGTLSLTGTDLEMEMVARVALV
QPHEPGATTVPARKFFDICRGLPEGAEIAVQLEGERMLVRSGRSRFSLSTLPAADFPNLD
DWQSEVEFTLPQATMKRLIEATQFSMAHQDVRYYLNGMLFETEGEELRTVATDGHRLAVC
SMPIGQSLPSHSVIVPRKGVIELMRMLDGGDNPLRVQIGSNNIRAHVGDFIFTSKLVDGR
FPDYRRVLPKNPDKHLEAGCDLLKQAFARAAILSNEKFRGVRLYVSENQLKITANNPEQE
EAEEILDVTYSGAEMEIGFNVSYVLDVLNALKCENVRMMLTDSVSSVQIEDAASQSAAYV
VMPMRL

Sequence of entity 2 (C, D), FASTA

>1UNN_2 DNA POLYMERASE IV (chains C, D)
HHHHHHVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQ
QTTQEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL

Primary citation

Structural Basis for Recruitment of Translesion DNA Polymerase Pol Iv/Dinb to the Beta-Clamp. Bunting, K.A., Roe, S.M., Pearl, L.H. EMBO J (2003) 22:5883. DOI 10.1093/EMBOJ/CDG568 · PubMed

Other PDB entries of the same protein (UniProt P0A988 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8PAY 1.21 Å, Structure of the E.coli DNA polymerase sliding clamp with a covalently bound peptide 2.
8PAT 1.45 Å, Structure of the E.coli DNA polymerase sliding clamp with a covalently bound peptide 3.
4K3L 1.5 Å, E. coli sliding clamp in complex with AcLF dipeptide
8CIY 1.54 Å, DNA-polymerase sliding clamp (DnaN) from Escherichia coli in complex with…
7AZ8 1.61 Å, DNA polymerase sliding clamp from Escherichia coli with peptide 43 bound
4MJR 1.62 Å, E. coli sliding clamp in complex with (S)-Carprofen
6FVM 1.63 Å, Mutant DNA polymerase sliding clamp from Escherichia coli with bound P7 peptide
3D1G 1.64 Å, Structure of a small molecule inhibitor bound to a DNA sliding clamp
1OK7 1.65 Å, A Conserved protein binding-site on Bacterial Sliding Clamps
7AZ7 1.65 Å, DNA polymerase sliding clamp from Escherichia coli with peptide 37 bound
4N96 1.7 Å, E. coli sliding clamp in complex with 6-nitroindazole
4N98 1.7 Å, E. coli sliding clamp in complex with 4'-fluorobiphenyl-4-carboxylic acid

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