Crystal structure of MBP-fused BIL1/BZR1 (21-90) in complex with double-stranded DNA contaning ATCACGTGAT. Determined by X-ray diffraction at 2.42 Å resolution. Released 7 Dec 2022.
Explore 7VN2 in 3D Show helices and sheets RCSB PDB PDBe
7VN2 contains 54 α-helices and 53 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 |
|---|---|---|---|
| β-strand | -342--338 | 5 | 11 |
| α-helix | -331--317 | 15 | |
| β-strand | -314--310 | 5 | 11 |
| α-helix | -305--297 | 9 | |
| β-strand | -289--285 | 5 | 11 |
| α-helix | -281--276 | 6 | |
| β-strand | -272 | 1 | 12 |
| α-helix | -271--269 | 3 | |
| α-helix | -265--262 | 4 | |
| β-strand | -259 | 1 | 13 |
| α-helix | -257--252 | 6 | |
| β-strand | -250--249 | 2 | 14 |
| β-strand | -246--245 | 2 | 14 |
| β-strand | -242--237 | 6 | 11 |
| β-strand | -234--230 | 5 | 15 |
| β-strand | -220 | 1 | 16 |
| α-helix | -216--208 | 9 | |
| β-strand | -203--201 | 3 | 15 |
| α-helix | -190--185 | 6 | |
| β-strand | -181--176 | 6 | 17 |
| β-strand | -173--166 | 8 | 17 |
| α-helix | -162--148 | 15 | |
| α-helix | -138--130 | 9 | |
| β-strand | -126--121 | 6 | 15 |
| α-helix | -119--117 | 3 | |
| α-helix | -116--111 | 6 | |
| β-strand | -106--103 | 4 | 15 |
| α-helix | -102--100 | 3 | |
| β-strand | -99 | 1 | 16 |
| β-strand | -98 | 1 | 18 |
| β-strand | -95 | 1 | 18 |
| α-helix | -94--93 | 2 | |
| α-helix | -91 | 1 | |
| β-strand | -90--89 | 2 | 19 |
| β-strand | -88--82 | 7 | 11 |
| β-strand | -81 | 1 | 12 |
| α-helix | -75--69 | 7 | |
| α-helix | -68--64 | 5 | |
| β-strand | -62 | 1 | 20 |
| α-helix | -61--52 | 10 | |
| β-strand | -47--46 | 2 | 11 |
| β-strand | -44 | 1 | 13 |
| α-helix | -43--37 | 7 | |
| α-helix | -33--22 | 12 | |
| β-strand | -20--19 | 2 | 19 |
| α-helix | -18--17 | 2 | |
| α-helix | -12-3 | 16 | |
| α-helix | 9-19 | 11 | |
| α-helix | 22-26 | 5 | |
| α-helix | 27-55 | 29 | |
| α-helix | 60 | 1 | |
| α-helix | 65-75 | 11 | |
| β-strand | 79-81 | 3 | 21 |
| β-strand | 84-87 | 4 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -341--338 | 4 | 1 |
| α-helix | -331--317 | 15 | |
| β-strand | -313--310 | 4 | 1 |
| α-helix | -305--298 | 8 | |
| α-helix | -297--295 | 3 | |
| β-strand | -289--285 | 5 | 1 |
| α-helix | -284--282 | 3 | |
| α-helix | -281--276 | 6 | |
| β-strand | -272 | 1 | 2 |
| α-helix | -271--269 | 3 | |
| α-helix | -265--262 | 4 | |
| β-strand | -259 | 1 | 3 |
| α-helix | -257--253 | 5 | |
| β-strand | -250--249 | 2 | 4 |
| β-strand | -246--245 | 2 | 4 |
| β-strand | -242--237 | 6 | 1 |
| β-strand | -234--230 | 5 | 5 |
| β-strand | -220 | 1 | 6 |
| α-helix | -216--207 | 10 | |
| β-strand | -203--201 | 3 | 5 |
| α-helix | -194--185 | 10 | |
| β-strand | -181--176 | 6 | 7 |
| β-strand | -173--166 | 8 | 7 |
| α-helix | -162--148 | 15 | |
| α-helix | -138--130 | 9 | |
| β-strand | -126--121 | 6 | 5 |
| α-helix | -119--117 | 3 | |
| α-helix | -116--111 | 6 | |
| β-strand | -106--103 | 4 | 5 |
| α-helix | -102--100 | 3 | |
| β-strand | -99 | 1 | 6 |
| β-strand | -98 | 1 | 8 |
| β-strand | -95 | 1 | 8 |
| α-helix | -91 | 1 | |
| β-strand | -90--89 | 2 | 9 |
| β-strand | -88--82 | 7 | 1 |
| β-strand | -81 | 1 | 2 |
| α-helix | -75--69 | 7 | |
| α-helix | -68--64 | 5 | |
| α-helix | -61--52 | 10 | |
| β-strand | -47--46 | 2 | 1 |
| β-strand | -44 | 1 | 3 |
| α-helix | -43--37 | 7 | |
| α-helix | -33--22 | 12 | |
| β-strand | -20--19 | 2 | 9 |
| α-helix | -18--17 | 2 | |
| α-helix | -12-4 | 17 | |
| α-helix | 9-21 | 13 | |
| α-helix | 22-26 | 5 | |
| α-helix | 27-54 | 28 | |
| α-helix | 65-75 | 11 | |
| β-strand | 79-80 | 2 | 10 |
| β-strand | 86-87 | 2 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1 | A, C | protein | 439 | Serratia sp. (strain FS14), Arabidopsis thaliana | P0AEX9 (AlphaFold model), Q8S307 (AlphaFold model) |
| DNA (5'-d(*tp*tp*ap*tp*cp*ap*cp*gp*tp*gp*ap*tp*ap*ap*a)-3') | E, G | DNA | 15 | synthetic construct |
>7VN2_1 Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1 (chains A, C) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAARRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGDYNLPKHCDNNEVLKA LCVEAGWVVEEDGTTYRKG
>7VN2_2 DNA (5'-D(*TP*TP*AP*TP*CP*AP*CP*GP*TP*GP*AP*TP*AP*AP*A)-3') (chains E, G) TTATCACGTGATAAA
Brassinosteroid-induced gene repression requires specific and tight promoter binding of BIL1/BZR1 via DNA shape readout. Nosaki, S., Mitsuda, N., Sakamoto, S. et al. Nat Plants (2022) 8:1440-1452. DOI 10.1038/s41477-022-01289-6 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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