1KNZ: Nonstructural RNA-binding Protein 34

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Determined by X-ray diffraction at 2.45 Å resolution. Released 17 Jan 2002.

Method: X-ray diffraction
Resolution: 2.45 Å
Organism: Simian rotavirus A/SA11
Chains: 12
Atoms: 9,555
Mol. weight: 153.22 kDa
Released: 17 Jan 2002

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

Secondary structure: helices and β-sheets

1KNZ contains 56 α-helices and 24 β-strands across 8 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: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	8-32	25
α-helix	39-56	18
α-helix	61-74	14
α-helix	79-89	11
α-helix	93-107	15
α-helix	114-123	10
β-strand	125-127	3	1
β-strand	136-138	3	1
α-helix	141-147	7
β-strand	152-155	4	2
α-helix	156-161	6

Chain B: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	6-32	27
α-helix	39-54	16
α-helix	61-74	14
α-helix	93-110	18
α-helix	115-123	9
β-strand	124-127	4	2
β-strand	134-139	6	2
α-helix	141-147	7
β-strand	152	1	1

Chain C: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	8-32	25
α-helix	39-56	18
α-helix	61-74	14
α-helix	79-89	11
α-helix	93-107	15
α-helix	114-121	8
β-strand	125-127	3	3
β-strand	136-138	3	3
α-helix	141-147	7
β-strand	152-153	2	4
α-helix	156-160	5

Chains D, J and N: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	6-32	27
α-helix	39-54	16
α-helix	61-74	14
α-helix	93-110	18
α-helix	115-123	9
β-strand	124-127	4	4
β-strand	136-139	4	4
α-helix	141-147	7
β-strand	152	1	3

Chain I: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	8-32	25
α-helix	39-56	18
α-helix	61-74	14
α-helix	79-89	11
α-helix	93-107	15
α-helix	114-123	10
β-strand	125-127	3	5
β-strand	136-138	3	5
α-helix	141-147	7
β-strand	152-153	2	6
α-helix	156-161	6

Chain M: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	8-32	25
α-helix	39-56	18
α-helix	61-74	14
α-helix	79-89	11
α-helix	93-107	15
α-helix	114-121	8
β-strand	125-127	3	7
β-strand	136-138	3	7
α-helix	141-147	7
β-strand	152-153	2	8
α-helix	156-161	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5'-r(upgpapcp*c)-3'	W, X, Y, Z	RNA	5
Nonstructural RNA-binding Protein 34	A, B, C, D, I, J, M, N	protein	164	Simian rotavirus A/SA11	P03536

Sequence of entity 1 (W, X, Y, Z), FASTA

>1KNZ_1 5'-R(*UP*GP*AP*CP*C)-3' (chains W, X, Y, Z)
UGACC

Sequence of entity 2 (A, B, C, D, I, J, M, N), FASTA

>1KNZ_2 Nonstructural RNA-binding Protein 34 (chains A, B, C, D, I, J, M, N)
LGSMESTQQMAVSIINSSFEAAVVAATSALENMGIEYDYQDIYSRVKNKFDFVMDDSGVK
NNPIGKAITIDQALNNKFGSAIRNRNWLADTSRPAKLDEDVNKLRMMLSSKGIDQKMRVL
NACFSVKRIPGKSSSIIKCTKLMRDKLERGEVEVDDSFVDEKME

Primary citation

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Deo, R.C., Groft, C.M., Rajashankar, K.R. et al. Cell (2002) 108:71-81. DOI 10.1016/S0092-8674(01)00632-8 · PubMed

Other PDB entries of the same protein (UniProt P03536), best resolution first:

1LJ2 2.38 Å, Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization

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