8TYC: Lassa GPC
Lassa GPC (strain Josiah) bound to rabbit polyclonal base-targeting antibody Base-1. Determined by electron microscopy at 3.3 Å resolution. Released 11 Sept 2024.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organisms
- Lassa virus, Oryctolagus cuniculus, Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
- Chains
- 8
- Atoms
- 10,628
- Mol. weight
- 255.62 kDa
- Ligands
- NAG
- Released
- 11 Sept 2024
Explore 8TYC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8TYC contains 63 α-helices and 75 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: 13 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 264-266 | 3 | |
| β-strand | 278-280 | 3 | 16 |
| α-helix | 282-284 | 3 | |
| β-strand | 285 | 1 | 2 |
| β-strand | 291-293 | 3 | 16 |
| α-helix | 295-298 | 4 | |
| α-helix | 299-302 | 4 | |
| α-helix | 308-325 | 18 | |
| α-helix | 327-329 | 3 | |
| α-helix | 335-344 | 10 | |
| α-helix | 347-358 | 12 | |
| β-strand | 363 | 1 | 17 |
| β-strand | 368-374 | 7 | 1 |
| β-strand | 380 | 1 | 1 |
| α-helix | 381-383 | 3 | |
| β-strand | 384-385 | 2 | 1 |
| α-helix | 386-387 | 2 | |
| β-strand | 388-389 | 2 | 17 |
| β-strand | 392-393 | 2 | 17 |
| α-helix | 394-395 | 2 | |
| α-helix | 396-399 | 4 | |
| α-helix | 400-419 | 20 | |
Chain A: 8 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 61-62 | 2 | 1 |
| β-strand | 66-72 | 7 | 1 |
| β-strand | 73 | 1 | 2 |
| α-helix | 75-78 | 4 | |
| β-strand | 84-87 | 4 | 3 |
| β-strand | 92-97 | 6 | 3 |
| β-strand | 101-108 | 8 | 3 |
| β-strand | 118 | 1 | 3 |
| α-helix | 120-126 | 7 | |
| α-helix | 131-142 | 12 | |
| α-helix | 150-152 | 3 | |
| β-strand | 153-156 | 4 | 3 |
| α-helix | 158-160 | 3 | |
| β-strand | 163-167 | 5 | 3 |
| α-helix | 183-194 | 12 | |
| α-helix | 199-202 | 4 | |
| β-strand | 219-226 | 8 | 3 |
| β-strand | 237 | 1 | 3 |
| α-helix | 239-245 | 7 | |
Chain b: 11 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 264-268 | 5 | |
| β-strand | 278-280 | 3 | 18 |
| α-helix | 282-284 | 3 | |
| β-strand | 285 | 1 | 5 |
| β-strand | 291-293 | 3 | 18 |
| α-helix | 295-298 | 4 | |
| α-helix | 299-302 | 4 | |
| α-helix | 308-325 | 18 | |
| α-helix | 327-329 | 3 | |
| α-helix | 335-344 | 10 | |
| α-helix | 348-358 | 11 | |
| β-strand | 363-374 | 12 | 4 |
| β-strand | 380 | 1 | 4 |
| α-helix | 381-383 | 3 | |
| β-strand | 384-388 | 5 | 4 |
| β-strand | 393 | 1 | 4 |
| α-helix | 394-395 | 2 | |
| α-helix | 400-419 | 20 | |
Chain B: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 61-62 | 2 | 4 |
| β-strand | 66-72 | 7 | 4 |
| β-strand | 73 | 1 | 5 |
| α-helix | 75-78 | 4 | |
| β-strand | 84-87 | 4 | 6 |
| β-strand | 92-97 | 6 | 6 |
| β-strand | 101-108 | 8 | 6 |
| α-helix | 120-126 | 7 | |
| α-helix | 131-141 | 11 | |
| α-helix | 150-152 | 3 | |
| β-strand | 153-155 | 3 | 6 |
| α-helix | 158-160 | 3 | |
| β-strand | 163-167 | 5 | 6 |
| α-helix | 184-194 | 11 | |
| α-helix | 199-202 | 4 | |
| β-strand | 219-224 | 6 | 6 |
| β-strand | 237 | 1 | 6 |
| α-helix | 239-244 | 6 | |
Chain c: 11 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 278-280 | 3 | 19 |
| α-helix | 282-284 | 3 | |
| β-strand | 285 | 1 | 8 |
| β-strand | 291-293 | 3 | 19 |
| α-helix | 295-298 | 4 | |
| α-helix | 299-302 | 4 | |
| α-helix | 308-325 | 18 | |
| α-helix | 327-329 | 3 | |
| α-helix | 335-344 | 10 | |
| α-helix | 347-358 | 12 | |
| β-strand | 363-374 | 12 | 7 |
| β-strand | 380 | 1 | 7 |
| α-helix | 381-383 | 3 | |
| β-strand | 384-389 | 6 | 7 |
| β-strand | 392-393 | 2 | 7 |
| α-helix | 394-395 | 2 | |
| α-helix | 397-399 | 3 | |
| α-helix | 400-419 | 20 | |
Chain C: 9 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 61-62 | 2 | 7 |
| β-strand | 66-72 | 7 | 7 |
| β-strand | 73 | 1 | 8 |
| α-helix | 75-80 | 6 | |
| β-strand | 84-87 | 4 | 9 |
| β-strand | 92-97 | 6 | 9 |
| β-strand | 101-108 | 8 | 9 |
| α-helix | 123-126 | 4 | |
| α-helix | 131-142 | 12 | |
| α-helix | 150-152 | 3 | |
| β-strand | 153-155 | 3 | 9 |
| α-helix | 158-160 | 3 | |
| β-strand | 163-167 | 5 | 9 |
| α-helix | 183-194 | 12 | |
| α-helix | 199-202 | 4 | |
| β-strand | 219-226 | 8 | 9 |
| β-strand | 237 | 1 | 9 |
| α-helix | 239-246 | 8 | |
| α-helix | 252-254 | 3 | |
Chain H: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17-23 | 7 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 11 |
| β-strand | 43-51 | 9 | 11 |
| β-strand | 58-59 | 2 | 11 |
| β-strand | 67-69 | 3 | 10 |
| β-strand | 76-82 | 7 | 10 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-93 | 6 | 11 |
| α-helix | 105 | 1 | |
| β-strand | 106-109 | 4 | 11 |
Chain L: 0 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 12 |
| β-strand | 11 | 1 | 13 |
| β-strand | 19-24 | 6 | 12 |
| β-strand | 34-39 | 6 | 14 |
| β-strand | 42-49 | 8 | 14 |
| β-strand | 52-53 | 2 | 14 |
| β-strand | 63-64 | 2 | 12 |
| β-strand | 68 | 1 | 15 |
| β-strand | 70 | 1 | 15 |
| β-strand | 71-75 | 5 | 12 |
| β-strand | 85-87 | 3 | 14 |
| β-strand | 102 | 1 | 14 |
| β-strand | 104 | 1 | 13 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glycoprotein G1 | A, B, C | protein | 259 | Lassa virus | P08669 (AlphaFold model) |
| Polyclonal antibody Base-1 heavy chain | H | protein | 108 | Oryctolagus cuniculus | |
| Polyclonal antibody Base-1 light chain | L | protein | 107 | Oryctolagus cuniculus | |
| Glycoprotein G2, 2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase… | a, b, c | protein | 406 | Lassa virus, Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) | P08669 (AlphaFold model), Q9WXS1 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>8TYC_1 Glycoprotein G1 (chains A, B, C)
MGQIVTFFQEVPHVIEEVMNIVLIALSVLAVLKGLYNFATCGLVGLVTFLLLCGRSCTTS
LYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNL
SDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHC
GTVANGVLQTFMRMAWGGSYIALDSGCGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIG
YLGLLSQRTRDIYISRRLL
Sequence of entity 2 (H), FASTA
>8TYC_2 Polyclonal antibody Base-1 heavy chain (chains H)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
Sequence of entity 3 (L), FASTA
>8TYC_3 Polyclonal antibody Base-1 light chain (chains L)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
Sequence of entity 4 (a, b, c), FASTA
>8TYC_4 Glycoprotein G2, 2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase fusion protein (chains a, b, c)
GTFTWTLSDSEGKDTPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFN
KQAIQRLKAPAQMSIQLINKAVNALINDQLIMKNHLRDIMCIPYCNYSKYWYLNHTTTGR
TSLPKCWLVSNGSYLNETHFSDDIEQQADNMITEMLQKEYMERQGGSGGSGGSGGSGGSE
KAAKAEEAARKMEELFKKHKIVAVLRANSVEEAIEKAVAVFAGGVHLIEITFTVPDADTV
IKALSVLKEKGAIIGAGTVTSVEQCRKAVESGAEFIVSPHLDEEISQFCKEKGVFYMPGV
MTPTELVKAMKLGHDILKLFPGEVVGPEFVKAMKGPFPNVKFVPTGGVDLDNVCEWFDAG
VLAVGVGDALVEGDPDEVREKAKEFVEKIRGCTEGSLEWSHPQFEK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Primary citation
Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses. Brouwer, P.J.M., Perrett, H.R., Beaumont, T. et al. Cell Rep (2024) 43:114708-114708. DOI 10.1016/j.celrep.2024.114708 · PubMed
Other PDB entries of the same protein (UniProt P08669 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9MJ1 1.9 Å, Native tagless Lassa virus spike complex bound at pH 8.0
- 9MHE 2.01 Å, Native tagless Lassa virus spike complex bound to ARN-75039 at pH 8.0
- 9MIV 2.02 Å, Native tagless Lassa virus spike complex pH 6.0
- 5OMI 2.56 Å, Crystal structure of GP2 from Lassa virus in a post fusion conformation
- 9MJ2 2.58 Å, Flag-tag Lassa virus spike complex at pH 6.0
- 4ZJF 2.6 Å, Crystal structure of GP1 - the receptor binding domain of Lassa virus
- 7S8H 2.7 Å, Structure of Lassa virus glycoprotein bound to Fab 18.5C and Fab 36.1F
- 9MIY 2.72 Å, Focused reconstruction of the transmembrane region of the Lassa virus spike complex
- 7UOV 2.75 Å, Native Lassa glycoprotein in complex with neutralizing antibodies 12.1F and 37.2D
- 7UOT 2.77 Å, Native Lassa glycoprotein in complex with neutralizing antibodies 8.9F and 37.2D
- 7TYV 2.8 Å, Structure of Lassa Virus glycoprotein (Josiah) bound to Fab 25.10C
- 8VCV 2.8 Å, Lineage IV Lassa virus glycoprotein (Josiah) in complex with rabbit polyclonal antibody…
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