chimera of the inactive ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin, with the double mutation K3528M and K3535I, fused to a proline-Rich-Domain (PRD) and profilin, bound to Latrunculin B-ADP-Mg-actin. Determined by X-ray diffraction at 1.69 Å resolution. Released 20 Sept 2023.
Explore 8BJH in 3D Show helices and sheets RCSB PDB PDBe
8BJH contains 49 α-helices and 48 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-38 | 4 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 2 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-144 | 8 | |
| β-strand | 150-155 | 6 | 3 |
| β-strand | 160-166 | 7 | 3 |
| β-strand | 169-170 | 2 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 3 |
| α-helix | 182-194 | 13 | |
| α-helix | 203-216 | 14 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 4 |
| β-strand | 247-250 | 4 | 4 |
| α-helix | 253-262 | 10 | |
| α-helix | 264-267 | 4 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-283 | 10 | |
| α-helix | 287-294 | 8 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 302-304 | 3 | |
| α-helix | 309-320 | 12 | |
| β-strand | 329-330 | 2 | 3 |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 369-373 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 468-470 | 3 | 5 |
| β-strand | 473-475 | 3 | 5 |
| α-helix | 476-478 | 3 | |
| α-helix | 481-485 | 5 | |
| α-helix | 490-503 | 14 | |
| β-strand | 505-509 | 5 | 6 |
| α-helix | 510-513 | 4 | |
| α-helix | 514-516 | 3 | |
| α-helix | 517-521 | 5 | |
| β-strand | 526-527 | 2 | 7 |
| β-strand | 537 | 1 | 8 |
| β-strand | 543 | 1 | 8 |
| β-strand | 547 | 1 | 9 |
| α-helix | 550-552 | 3 | |
| α-helix | 555-558 | 4 | |
| α-helix | 561-573 | 13 | |
| β-strand | 578-581 | 4 | 9 |
| β-strand | 583-584 | 2 | 10 |
| α-helix | 586-590 | 5 | |
| α-helix | 591-595 | 5 | |
| β-strand | 599 | 1 | 11 |
| α-helix | 600-602 | 3 | |
| β-strand | 603-605 | 3 | 10 |
| β-strand | 610-614 | 5 | 10 |
| β-strand | 615 | 1 | 11 |
| β-strand | 623-631 | 9 | 10 |
| β-strand | 634-643 | 10 | 10 |
| β-strand | 646-649 | 4 | 10 |
| β-strand | 651-654 | 4 | 9 |
| α-helix | 660 | 1 | |
| β-strand | 661 | 1 | 9 |
| β-strand | 662-663 | 2 | 7 |
| β-strand | 668-674 | 7 | 6 |
| α-helix | 675-677 | 3 | |
| α-helix | 729-742 | 14 | |
| α-helix | 744-745 | 2 | |
| α-helix | 764-766 | 3 | |
| β-strand | 770-773 | 4 | 6 |
| α-helix | 776-779 | 4 | |
| α-helix | 791-794 | 4 | |
| β-strand | 796-797 | 2 | 6 |
| β-strand | 803-805 | 3 | 6 |
| α-helix | 808-820 | 13 | |
| β-strand | 823-824 | 2 | 6 |
| α-helix | 848-860 | 13 | |
| α-helix | 896-899 | 4 | |
| α-helix | 906-913 | 8 | |
| β-strand | 918-925 | 8 | 12 |
| β-strand | 931-935 | 5 | 12 |
| α-helix | 941-943 | 3 | |
| α-helix | 946-953 | 8 | |
| α-helix | 959-961 | 3 | |
| β-strand | 965-967 | 3 | 12 |
| β-strand | 970-978 | 9 | 12 |
| β-strand | 986-991 | 6 | 12 |
| β-strand | 1001-1006 | 6 | 12 |
| β-strand | 1010-1016 | 7 | 12 |
| α-helix | 1022-1038 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle, intermediate form | A | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Putative Adenylate cyclase,Profilin-1 | B | protein | 591 | Vibrio nigripulchritudo, Homo sapiens | A0A9P1NJI6, P07737 (AlphaFold model) |
>8BJH_1 Actin, alpha skeletal muscle, intermediate form (chains A) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>8BJH_2 Putative Adenylate cyclase,Profilin-1 (chains B) GPGSQEATPNQDGSHKTYQSRDLVLEPIQHPKSIELGMPEVDQSVLAEVAERENVIIGVR PVDEKSKSLIASKMYSSMGLFVKAISSDWGPMSGFIPVDQSFAKASARRDLEKFNEYAEQ SILSGNAVSANLYLNQVRIEELVSKYESLTPLELDVDSGMYKTTATNGDQTIPFFLNKVT VDDKELWQVHYLREGELAPFKVIGDPVSKQPMTADYDLLTVMYTYGDLGPQDKVKQPLTW EQWKESVTYEDLSPKYKARYDNQALYEKQDGASLGMVSDRLKELKDVINTSLGRTDGLEM VHHGADDANPYAVMADNFPATFFVPKHFFDDDGLGEGKGSIQTYFNVNEQGAVVIQNPQE FSNFQQVAINASYRASLNDKWNSGLDSPLFTTKRKLSHDYLDARDEVAKKLGLTESSKLN GLGERQTMSPAQNSDVNTWARVDVSPPPPPGGAGWNAYIDNLMADGTCQDAAIVGYKDSP SVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLR TKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
| ID | Name | Formula | Copies |
|---|---|---|---|
| PEO | Hydrogen peroxide | H2 O2 | 8 |
| LAB | Latrunculin B | C20 H29 N O5 S | 1 |
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (SO4, GOL, TRS, PEG) are not listed.
Functional and structural insights into the multi-step activation and catalytic mechanism of bacterial ExoY nucleotidyl cyclase toxins bound to actin-profilin. Teixeira-Nunes, M., Retailleau, P., Raoux-Barbot, D. et al. PLoS Pathog (2023) 19:e1011654-e1011654. DOI 10.1371/journal.ppat.1011654 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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