T3 SAM lyase in complex with S-adenosylmethionine synthase. Determined by electron microscopy at 2.8 Å resolution. Released 23 Aug 2023.
Explore 8BB1 in 3D Show helices and sheets RCSB PDB PDBe
8BB1 contains 100 α-helices and 116 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-10 | 8 | 1 |
| α-helix | 15-33 | 19 | |
| β-strand | 38-45 | 8 | 2 |
| β-strand | 49-57 | 9 | 2 |
| α-helix | 64-75 | 12 | |
| α-helix | 80-82 | 3 | |
| β-strand | 90-98 | 9 | 2 |
| α-helix | 111-113 | 3 | |
| α-helix | 114-115 | 2 | |
| β-strand | 116 | 1 | 3 |
| β-strand | 120-127 | 8 | 4 |
| β-strand | 130 | 1 | 5 |
| α-helix | 136-154 | 19 | |
| β-strand | 160-173 | 14 | 1 |
| β-strand | 176-189 | 14 | 1 |
| α-helix | 195-202 | 8 | |
| α-helix | 203-207 | 5 | |
| α-helix | 208-210 | 3 | |
| β-strand | 221-224 | 4 | 1 |
| α-helix | 234-236 | 3 | |
| β-strand | 240-241 | 2 | 2 |
| α-helix | 246-250 | 5 | |
| α-helix | 252-254 | 3 | |
| β-strand | 265 | 1 | 2 |
| α-helix | 270-287 | 18 | |
| β-strand | 291 | 1 | 6 |
| β-strand | 293-300 | 8 | 4 |
| β-strand | 302 | 1 | 3 |
| β-strand | 309-313 | 5 | 4 |
| β-strand | 318 | 1 | 6 |
| α-helix | 322-332 | 11 | |
| α-helix | 337-344 | 8 | |
| α-helix | 353-355 | 3 | |
| α-helix | 366-368 | 3 | |
| α-helix | 373-379 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| α-helix | 7 | 1 | |
| β-strand | 11-15 | 5 | 23 |
| α-helix | 24-40 | 17 | |
| α-helix | 42-45 | 4 | |
| β-strand | 47-54 | 8 | 23 |
| β-strand | 57 | 1 | 24 |
| β-strand | 66 | 1 | 24 |
| β-strand | 69-75 | 7 | 23 |
| α-helix | 78-86 | 9 | |
| α-helix | 87-91 | 5 | |
| β-strand | 97-100 | 4 | 23 |
| β-strand | 107-111 | 5 | 23 |
| β-strand | 119-122 | 4 | 23 |
| β-strand | 126-129 | 4 | 23 |
| α-helix | 130-131 | 2 | |
| α-helix | 135-136 | 2 | |
| β-strand | 141-142 | 2 | 23 |
| β-strand | 148-152 | 5 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| S-adenosylmethionine synthase | A, B, C, D | protein | 384 | Escherichia coli | P0A817 (AlphaFold model) |
| S-Adenosylmethionine lyase | E, F, G, H | protein | 158 | Enterobacteria phage T3 | P07693 |
>8BB1_1 S-adenosylmethionine synthase (chains A, B, C, D) MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTS AWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQ GLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVG IDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDC GLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVS YAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGH FGREHFPWEKTDKAQLLRDAAGLK
>8BB1_2 S-Adenosylmethionine lyase (chains E, F, G, H) MIFTKEPANVFYVLVSAFRSNLCDEVNMSRHRHMVSTLRAAPGLYGSVESTDLTGCYREA ISSAPTEEKTVRVRCKDKAQALNVARLACNEWEQDCVLVYKSQTHTAGLVYAKGIDGYKA ERLPGSFQEVPKGAPLQGCFTIDEFGRRWQVQHHHHHH
Phage T3 overcomes the BREX defense through SAM cleavage and inhibition of SAM synthesis by SAM lyase. Andriianov, A., Triguis, S., Drobiazko, A. et al. Cell Rep (2023) 42:112972-112972. DOI 10.1016/j.celrep.2023.112972 · PubMed
Other PDB entries of the same protein (UniProt P0A817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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