8EAW: Capsid protein

An asymmetric disk assembly formed by tandem dimers of the tobacco mosaic viral capsid protein (TMV). Determined by X-ray diffraction at 2.8 Å resolution. Released 1 Mar 2023.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Tobacco mosaic virus (vulgare)
Chains: 17
Atoms: 38,318
Mol. weight: 603.44 kDa
Released: 1 Mar 2023

Explore 8EAW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8EAW contains 257 α-helices and 228 β-strands across 17 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.

Chains a and d: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	1
α-helix	7-13	7
β-strand	17-18	2	2
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	2
β-strand	57	1	3
β-strand	60	1	3
α-helix	61-63	3
β-strand	68-70	3	2
α-helix	76-86	11
α-helix	104-133	30
β-strand	138-139	2	2
α-helix	141-148	8
β-strand	151-152	2	1
β-strand	167	1	4
α-helix	172-178	7
β-strand	182-183	2	5
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	5
α-helix	226-228	3
β-strand	233-235	3	5
α-helix	241-251	11
α-helix	277-299	23
β-strand	303-304	2	5
α-helix	306-312	7
α-helix	315-316	2
β-strand	317	1	4

Chain b: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	6
α-helix	7-13	7
β-strand	17-18	2	7
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	7
β-strand	57	1	8
β-strand	60	1	8
α-helix	61-63	3
β-strand	68-70	3	7
α-helix	76-86	11
α-helix	106-133	28
β-strand	138-139	2	7
α-helix	141-148	8
β-strand	151-152	2	6
β-strand	167	1	9
α-helix	172-178	7
β-strand	182-183	2	10
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	10
α-helix	226-228	3
β-strand	233-235	3	10
α-helix	241-251	11
α-helix	277-299	23
β-strand	303-304	2	10
α-helix	306-312	7
α-helix	315-316	2
β-strand	317	1	9

Chain c: 15 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	11
α-helix	7-13	7
β-strand	17-18	2	12
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	12
α-helix	61-63	3
β-strand	68-70	3	12
α-helix	76-86	11
α-helix	106-133	28
β-strand	138-139	2	12
α-helix	141-147	7
β-strand	151-152	2	11
β-strand	167	1	13
α-helix	172-178	7
β-strand	182-183	2	14
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	14
α-helix	226-228	3
β-strand	233-235	3	14
α-helix	241-251	11
α-helix	277-298	22
β-strand	303-304	2	14
α-helix	306-313	8
α-helix	315-316	2
β-strand	317	1	13

Chain e: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	20
α-helix	7-13	7
β-strand	17-18	2	21
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	21
β-strand	57	1	22
β-strand	60	1	22
α-helix	61-63	3
β-strand	68-70	3	21
α-helix	76-86	11
α-helix	104-134	31
β-strand	138-139	2	21
α-helix	141-148	8
β-strand	151-152	2	20
β-strand	167	1	23
α-helix	172-178	7
β-strand	182-183	2	24
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	24
α-helix	226-228	3
β-strand	233-235	3	24
α-helix	241-251	11
α-helix	277-299	23
β-strand	303-304	2	24
α-helix	306-312	7
α-helix	315-316	2
β-strand	317	1	23

Chain f: 15 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	25
α-helix	7-13	7
β-strand	17-18	2	26
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	26
α-helix	61-63	3
β-strand	68-70	3	26
α-helix	76-86	11
α-helix	104-133	30
β-strand	138-139	2	26
α-helix	141-148	8
β-strand	151-152	2	25
β-strand	167-168	2	27
α-helix	172-178	7
β-strand	182-183	2	28
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	28
α-helix	226-228	3
β-strand	233-235	3	28
α-helix	241-251	11
α-helix	277-298	22
β-strand	303-304	2	28
α-helix	306-313	8
α-helix	315	1
β-strand	316-317	2	27

Chain g: 16 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	29
α-helix	7-13	7
β-strand	17-18	2	30
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	30
β-strand	57	1	31
β-strand	60	1	31
α-helix	61-63	3
β-strand	68-70	3	30
α-helix	76-86	11
α-helix	106-133	28
β-strand	138-139	2	30
α-helix	141-148	8
β-strand	151-152	2	29
β-strand	167-168	2	32
α-helix	169	1
α-helix	172-178	7
β-strand	182-183	2	33
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	33
α-helix	226-228	3
β-strand	233-235	3	33
α-helix	241-251	11
α-helix	277-298	22
β-strand	303-304	2	33
α-helix	306-313	8
α-helix	315	1
β-strand	316-317	2	32

Chain h: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	34
α-helix	7-13	7
β-strand	17-18	2	35
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	35
β-strand	57	1	36
β-strand	60	1	36
α-helix	61-63	3
β-strand	68-70	3	35
α-helix	76-86	11
α-helix	106-133	28
β-strand	138-139	2	35
α-helix	141-148	8
β-strand	151-152	2	34
β-strand	167	1	37
α-helix	172-178	7
β-strand	182-183	2	38
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	38
α-helix	226-228	3
β-strand	233-235	3	38
α-helix	241-251	11
α-helix	277-299	23
β-strand	303-304	2	38
α-helix	306-313	8
α-helix	315-316	2
β-strand	317	1	37

Chains i and k: 15 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	39
α-helix	7-13	7
β-strand	17-18	2	40
α-helix	20-30	11
α-helix	38-50	13
β-strand	53	1	40
α-helix	61-63	3
β-strand	68-70	3	40
α-helix	76-86	11
α-helix	104-133	30
β-strand	138-139	2	40
α-helix	141-148	8
β-strand	151-152	2	39
β-strand	167	1	41
α-helix	172-178	7
β-strand	182-183	2	42
α-helix	185-195	11
α-helix	203-215	13
β-strand	218	1	42
α-helix	226-228	3
β-strand	233-235	3	42
α-helix	241-251	11
α-helix	277-298	22
β-strand	303-304	2	42
α-helix	306-313	8
α-helix	315-316	2
β-strand	317	1	41

6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Capsid protein	a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q	protein	323	Tobacco mosaic virus (vulgare)	P69687

Sequence of entity 1 (a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q), FASTA

>8EAW_1 Capsid protein (chains a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q)
SYSITTPSQFVFLSSAWADPIELINLCTNALGNQFQTQQARTVVQRQFSEVWKPSPQVTV
RFPDSDFKVYRYNAVLDPLVTALLGAFDTRNRIIEVENQANPTTAETLDATRRVDDATVA
IRCAINNLIVELIRGTGSYNRSSFESSSGLVWTSGPATGGGEGGGSYSITTPSQFVFLSS
AWADPIELINLCTNALGNQFQTQQARTVVQRQFSEVWKPSPQVTVRFPDSDFKVYRYNAV
LDPLVTALLGAFDTRNRIIEVENQANPTTAETLDATRRVDDATVAIRCAINNLIVELIRG
TGSYNRSSFESSSGLVWTSGPAT

Primary citation

A Membrane-Associated Light-Harvesting Model is Enabled by Functionalized Assemblies of Gene-Doubled TMV Proteins. Dai, J., Wilhelm, K.B., Bischoff, A.J. et al. Small (2023) 19:e2207805-e2207805. DOI 10.1002/smll.202207805 · PubMed

Other PDB entries of the same protein (UniProt P69687), best resolution first:

6SAE 1.9 Å, Cryo-EM structure of TMV in water
6R7M 1.92 Å, Tobacco Mosaic Virus (TMV)
6SAG 2.0 Å, Cryo-EM structure of TMV with Ca2+ at low pH
6I5A 2.3 Å, Tobacco Mosaic Virus
6RLP 2.3 Å, Cryo-EM reconstruction of TMV coat protein
1EI7 2.45 Å, Tmv coat protein refined from the 4-layer aggregate
2TMV 2.9 Å, Visualization of protein-nucleic acid interactions in a virus. Refined structure of…
6X0Q 3.0 Å, A Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101H coordinated with heme
6X0R 3.0 Å, A Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101H
3KML 3.01 Å, Circular Permutant of the Tobacco Mosaic Virus
4GQH 3.06 Å, The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray…
3J06 3.3 Å, CryoEM Helical Reconstruction of TMV

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