7VN7: MBP-fused BIL1/BZR1

Crystal structure of MBP-fused BIL1/BZR1 (21-90) in complex with double-stranded DNA contaning GACACGTGTC. Determined by X-ray diffraction at 2.11 Å resolution. Released 7 Dec 2022.

Method: X-ray diffraction
Resolution: 2.11 Å
Organisms: Serratia sp. (strain FS14), Arabidopsis thaliana, synthetic construct
Chains: 8
Atoms: 15,251
Mol. weight: 214.17 kDa
Released: 7 Dec 2022

Explore 7VN7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7VN7 contains 108 α-helices and 109 β-strands across 4 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: 26 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	-342--338	5	22
α-helix	-331--317	15
β-strand	-314--310	5	22
α-helix	-305--296	10
β-strand	-289--285	5	22
α-helix	-284--282	3
α-helix	-281--276	6
β-strand	-272	1	23
α-helix	-271--270	2
β-strand	-269	1	24
α-helix	-265--262	4
β-strand	-259	1	25
α-helix	-257--252	6
β-strand	-250--249	2	24
β-strand	-246--245	2	24
β-strand	-242--237	6	22
β-strand	-234--230	5	26
β-strand	-220	1	27
α-helix	-216--207	10
β-strand	-203--201	3	26
α-helix	-194--187	8
β-strand	-181--176	6	28
β-strand	-173--166	8	28
α-helix	-162--148	15
α-helix	-138--130	9
β-strand	-126--121	6	26
α-helix	-119--117	3
α-helix	-116--111	6
β-strand	-106--103	4	26
α-helix	-102--100	3
β-strand	-99	1	27
β-strand	-98	1	29
β-strand	-95	1	29
α-helix	-91	1
β-strand	-90--89	2	30
β-strand	-88--82	7	22
β-strand	-81	1	23
α-helix	-75--70	6
α-helix	-69--64	6
α-helix	-61--52	10
β-strand	-47--46	2	22
β-strand	-44	1	25
α-helix	-43--37	7
α-helix	-33--22	12
β-strand	-20--19	2	30
α-helix	-18--17	2
α-helix	-12-4	17
α-helix	9-21	13
α-helix	22-26	5
α-helix	27-55	29
α-helix	65-75	11
β-strand	79-80	2	31
β-strand	86-87	2	31

Chain B: 30 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	-342--338	5	32
α-helix	-331--317	15
β-strand	-314--310	5	32
α-helix	-305--297	9
β-strand	-289--285	5	32
α-helix	-284--282	3
α-helix	-281--276	6
β-strand	-272	1	33
α-helix	-271--270	2
β-strand	-269	1	34
α-helix	-265--262	4
β-strand	-259	1	35
α-helix	-257--252	6
β-strand	-250--249	2	34
β-strand	-246--245	2	34
β-strand	-242--237	6	32
β-strand	-234--230	5	36
β-strand	-220	1	37
α-helix	-217--208	10
β-strand	-203--201	3	36
α-helix	-194--192	3
α-helix	-190--185	6
β-strand	-179--176	4	38
β-strand	-173--167	7	38
α-helix	-162--148	15
α-helix	-138--130	9
β-strand	-126--121	6	36
α-helix	-119--117	3
α-helix	-116--111	6
β-strand	-106--103	4	36
α-helix	-102--100	3
β-strand	-99	1	37
β-strand	-98	1	39
β-strand	-95	1	39
α-helix	-94--93	2
α-helix	-91	1
β-strand	-90--89	2	40
β-strand	-88--82	7	32
β-strand	-81	1	33
α-helix	-75--70	6
α-helix	-69--64	6
α-helix	-61--52	10
β-strand	-47--46	2	32
β-strand	-44	1	35
α-helix	-43--37	7
α-helix	-33--22	12
β-strand	-20--19	2	40
α-helix	-18--17	2
α-helix	-12-3	16
α-helix	9-20	12
α-helix	22-26	5
α-helix	27	1
α-helix	28-32	5
α-helix	37-53	17
α-helix	65-75	11
β-strand	79-80	2	41
β-strand	86-87	2	41

Chain C: 26 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	-347	1	1
β-strand	-342--338	5	2
α-helix	-331--317	15
β-strand	-314--310	5	2
α-helix	-305--297	9
β-strand	-293	1	1
β-strand	-289--285	5	2
α-helix	-284--282	3
α-helix	-281--276	6
β-strand	-272	1	3
α-helix	-271--269	3
α-helix	-265--262	4
β-strand	-259	1	4
α-helix	-257--252	6
β-strand	-250--249	2	5
β-strand	-246--245	2	5
β-strand	-242--237	6	2
β-strand	-234--230	5	6
β-strand	-220	1	7
α-helix	-216--208	9
β-strand	-203--201	3	6
α-helix	-194--185	10
β-strand	-181--176	6	8
β-strand	-173--166	8	8
α-helix	-162--148	15
α-helix	-138--130	9
β-strand	-126--121	6	6
α-helix	-119--117	3
α-helix	-116--111	6
β-strand	-106--103	4	6
α-helix	-102--100	3
β-strand	-99	1	7
β-strand	-98	1	9
β-strand	-95	1	9
α-helix	-91	1
β-strand	-90--89	2	10
β-strand	-88--82	7	2
β-strand	-81	1	3
α-helix	-75--69	7
α-helix	-68--64	5
α-helix	-61--52	10
β-strand	-47--46	2	2
β-strand	-44	1	4
α-helix	-43--37	7
α-helix	-33--22	12
β-strand	-20--19	2	10
α-helix	-18--17	2
α-helix	-12-3	16
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	11
β-strand	86-87	2	11

Chain D: 26 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	-342--338	5	12
α-helix	-331--317	15
β-strand	-314--310	5	12
α-helix	-305--298	8
β-strand	-289--285	5	12
α-helix	-284--282	3
α-helix	-281--276	6
β-strand	-272	1	13
α-helix	-271--270	2
β-strand	-269	1	14
α-helix	-265--262	4
β-strand	-259	1	15
α-helix	-257--252	6
β-strand	-250--249	2	14
β-strand	-246--245	2	14
β-strand	-242--237	6	12
β-strand	-234--230	5	16
β-strand	-220	1	17
α-helix	-216--208	9
β-strand	-203--201	3	16
α-helix	-194--185	10
β-strand	-181--176	6	18
β-strand	-173--166	8	18
α-helix	-162--148	15
α-helix	-138--130	9
β-strand	-126--121	6	16
α-helix	-119--117	3
α-helix	-116--111	6
β-strand	-106--103	4	16
α-helix	-102--100	3
β-strand	-99	1	17
β-strand	-98	1	19
β-strand	-95	1	19
α-helix	-91	1
β-strand	-90--89	2	20
β-strand	-88--82	7	12
β-strand	-81	1	13
α-helix	-75--69	7
α-helix	-68--64	5
α-helix	-61--52	10
β-strand	-47--46	2	12
β-strand	-44	1	15
α-helix	-43--37	7
α-helix	-33--22	12
β-strand	-20--19	2	20
α-helix	-18--17	2
α-helix	-12-3	16
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	21
β-strand	86-87	2	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1	A, B, C, D	protein	439	Serratia sp. (strain FS14), Arabidopsis thaliana	P0AEX9 (AlphaFold model), Q8S307 (AlphaFold model)
DNA (5'-d(tptpgpapcpapcpgptpgptpcpapap*a)-3')	E, F, G, H	DNA	15	synthetic construct

Sequence of entity 1 (A, B, C, D), FASTA

>7VN7_1 Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1 (chains A, B, C, D)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNAARRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGDYNLPKHCDNNEVLKA
LCVEAGWVVEEDGTTYRKG

Sequence of entity 2 (E, F, G, H), FASTA

>7VN7_2 DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3') (chains E, F, G, H)
TTGACACGTGTCAAA

Primary citation

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:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

Browse structure collections

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