4N0O: Replicase polyprotein 1ab

Complex structure of Arterivirus nonstructural protein 10 (helicase) with DNA. Determined by X-ray diffraction at 2.65 Å resolution. Released 8 Jan 2014.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Equine arteritis virus
Chains: 8
Atoms: 12,998
Mol. weight: 192.02 kDa
Ligands: CA, ZN
Released: 8 Jan 2014

Explore 4N0O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N0O contains 58 α-helices and 100 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: 17 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	1
β-strand	20-21	2	1
α-helix	26-28	3
β-strand	35-36	2	1
α-helix	46-48	3
β-strand	49	1	2
β-strand	53	1	2
α-helix	72-79	8
β-strand	91	1	3
β-strand	96-97	2	4
β-strand	102-104	3	5
β-strand	109-111	3	5
β-strand	119-120	2	4
β-strand	122	1	5
β-strand	127	1	3
β-strand	132	1	5
α-helix	133-135	3
α-helix	143-152	10
β-strand	154-157	4	6
α-helix	164-172	9
β-strand	179-182	4	6
α-helix	186-198	13
β-strand	204-205	2	6
α-helix	216-218	3
β-strand	223-226	4	6
β-strand	236-240	5	6
α-helix	242-244	3
α-helix	247-255	9
β-strand	260-263	4	6
α-helix	268-270	3
α-helix	278-280	3
α-helix	282-284	3
β-strand	286-287	2	6
β-strand	293	1	7
α-helix	299-303	5
β-strand	313	1	7
β-strand	320-323	4	8
β-strand	333-336	4	8
β-strand	347-348	2	8
α-helix	350-352	3
β-strand	357-363	7	8
α-helix	372-376	5
β-strand	382-389	8	8
α-helix	396-399	4

Chain C: 13 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	9
α-helix	26-28	3
β-strand	35-37	3	9
α-helix	46-48	3
β-strand	49	1	10
β-strand	53	1	10
α-helix	72-79	8
β-strand	87-88	2	11
β-strand	101-104	4	12
β-strand	109-112	4	12
β-strand	121	1	12
β-strand	129-130	2	11
β-strand	133	1	12
α-helix	143-150	8
β-strand	154-157	4	13
α-helix	164-173	10
β-strand	179-182	4	13
α-helix	186-198	13
β-strand	204	1	13
β-strand	223-226	4	13
β-strand	236-240	5	13
α-helix	247-255	9
β-strand	259-263	5	13
α-helix	282-284	3
β-strand	286-287	2	13
β-strand	293	1	14
α-helix	299-305	7
β-strand	313	1	14
β-strand	320-322	3	15
β-strand	333-336	4	15
β-strand	346-348	3	15
α-helix	349-351	3
β-strand	357-363	7	15
α-helix	372-378	7
β-strand	382-389	8	15
α-helix	394-395	2
α-helix	396-400	5

Chain E: 15 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	13-15	3	16
β-strand	20-21	2	16
β-strand	35-37	3	16
α-helix	46-48	3
α-helix	55-57	3
α-helix	65-68	4
α-helix	72-79	8
β-strand	89	1	17
β-strand	91	1	18
β-strand	97	1	18
β-strand	101-104	4	19
β-strand	109-112	4	19
β-strand	119	1	18
β-strand	122	1	19
β-strand	129	1	17
β-strand	133	1	19
α-helix	134-136	3
α-helix	143-152	10
β-strand	154-157	4	20
α-helix	164-172	9
β-strand	179-182	4	20
α-helix	186-197	12
β-strand	204	1	20
β-strand	223-226	4	20
β-strand	236-240	5	20
α-helix	242-244	3
α-helix	247-253	7
β-strand	259-263	5	20
α-helix	279-282	4
β-strand	286-287	2	20
β-strand	293	1	21
α-helix	299-304	6
β-strand	313	1	21
β-strand	320-323	4	22
β-strand	333-336	4	22
β-strand	346-348	3	22
α-helix	349-351	3
β-strand	357-363	7	22
α-helix	372-378	7
β-strand	382-389	8	22
α-helix	395-399	5

Chain G: 13 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	13-14	2	23
β-strand	20-21	2	23
α-helix	26-29	4
β-strand	36-37	2	23
α-helix	46-48	3
β-strand	49	1	24
β-strand	53	1	24
α-helix	72-79	8
β-strand	87	1	25
β-strand	103	1	26
β-strand	110	1	26
β-strand	131	1	25
α-helix	143-150	8
β-strand	154-157	4	27
α-helix	164-173	10
β-strand	179-182	4	27
α-helix	187-199	13
β-strand	203-205	3	27
β-strand	223-226	4	27
β-strand	236-239	4	27
α-helix	249-254	6
β-strand	259-263	5	27
α-helix	282-284	3
β-strand	286-287	2	27
β-strand	293	1	28
α-helix	299-305	7
β-strand	313	1	28
β-strand	320-323	4	29
β-strand	333-336	4	29
α-helix	339-341	3
β-strand	347-348	2	29
α-helix	349-351	3
β-strand	357-363	7	29
α-helix	372-380	9
β-strand	382-389	8	29
α-helix	394-399	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Replicase polyprotein 1ab	A, C, E, G	protein	423	Equine arteritis virus	P19811 (AlphaFold model)
DNA	B, D, F, H	DNA	7

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

>4N0O_1 Replicase polyprotein 1ab (chains A, C, E, G)
MGSSHHHHHSSGENLYFQGHMSAVCTVCGAAPVAKSACGGWFCGNCVPYHAGHCHTTSLF
ANCGHDIMYRSTYCTMCEGSPKQMVPKVPHPILDHLLCHIDYGSKEELTLVVADGRTTSP
PGRYKVGHKVVAVVADVGGNIVFGCGPGSHIAVPLQDTLKGVVVNKALKNAAASEYVEGP
PGSGKTFHLVKDVLAVVGSATLVVPTHASMLDCINKLKQAGADPYFVVPKYTVLDFPRPG
SGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILTQGRVKGYGDLNQLGCVGPASVPRN
LWLRHFVSLEPLRVCHRFGAAVCDLIKGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYH
KDRGLGHRTIDSIQGCTFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLL
KFT

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

>4N0O_2 DNA (chains B, D, F, H)
TTTTTTT

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	7
ZN	Zinc ion	Zn	12

Primary citation

Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase. Deng, Z., Lehmann, K.C., Li, X. et al. Nucleic Acids Res (2014) 42:3464-3477. DOI 10.1093/nar/gkt1310 · PubMed

Other PDB entries of the same protein (UniProt P19811 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4IUM 1.45 Å, Equine arteritis virus papain-like protease 2 (PLP2) covalently bound to ubiquitin
1MBM 2.0 Å, NSP4 proteinase from Equine Arteritis Virus
4N0N 2.0 Å, Crystal structure of Arterivirus nonstructural protein 10 (helicase)
5HBZ 3.1 Å, Structure of EAV NSP11 K170A mutant at 3.10A
5HC1 3.1 Å, Structure of EAV NSP11 H141A mutant at 3.10A
5F17 3.2 Å, Structure of EAV NSP11 K170A mutant at 3.19A
2L8K NMR Structure of the Arterivirus nonstructural protein 7 alpha (nsp7 alpha)

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