[English] 日本語
Yorodumi
- PDB-7vn7: Crystal structure of MBP-fused BIL1/BZR1 (21-90) in complex with ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7vn7
TitleCrystal structure of MBP-fused BIL1/BZR1 (21-90) in complex with double-stranded DNA contaning GACACGTGTC
Components
  • DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
  • Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
KeywordsTRANSCRIPTION / Transcription factor-DNA complex
Function / homology
Function and homology information


plant ovule development / seed development / brassinosteroid mediated signaling pathway / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / periplasmic space / DNA-binding transcription factor activity ...plant ovule development / seed development / brassinosteroid mediated signaling pathway / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / periplasmic space / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / DNA-templated transcription / regulation of DNA-templated transcription / DNA binding / nucleus / cytosol
Similarity search - Function
BZR family / BES1/BZR1 plant transcription factor, N-terminal / BES1/BZR1 plant transcription factor, N-terminal / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain
Similarity search - Domain/homology
alpha-maltose / DNA / DNA (> 10) / Maltodextrin-binding protein / Protein BRASSINAZOLE-RESISTANT 1
Similarity search - Component
Biological speciesSerratia sp. (bacteria)
Arabidopsis thaliana (thale cress)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.11 Å
AuthorsNosaki, S. / Tanokura, M. / Miyakawa, T.
Funding support Japan, 2items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)17H05835, 19H04855, 19K23658, 21H02114 Japan
Japan Agency for Medical Research and Development (AMED)JP20am0101077 Japan
CitationJournal: Nat.Plants / Year: 2022
Title: Brassinosteroid-induced gene repression requires specific and tight promoter binding of BIL1/BZR1 via DNA shape readout.
Authors: Nosaki, S. / Mitsuda, N. / Sakamoto, S. / Kusubayashi, K. / Yamagami, A. / Xu, Y. / Bui, T.B.C. / Terada, T. / Miura, K. / Nakano, T. / Tanokura, M. / Miyakawa, T.
History
DepositionOct 10, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 7, 2022Provider: repository / Type: Initial release
Revision 1.1Dec 28, 2022Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 11, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
C: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
D: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
G: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
H: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
A: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
B: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
E: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
F: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)214,16524
Polymers212,0518
Non-polymers2,11416
Water5,386299
1
C: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
D: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
G: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
H: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,20714
Polymers106,0264
Non-polymers1,18110
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11410 Å2
ΔGint8 kcal/mol
Surface area40070 Å2
MethodPISA
2
A: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
B: Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1
E: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
F: DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,95910
Polymers106,0264
Non-polymers9336
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9510 Å2
ΔGint-6 kcal/mol
Surface area41650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.437, 93.211, 112.240
Angle α, β, γ (deg.)90.000, 100.363, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

-
Components

#1: Protein
Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1 / Protein BIN2 SUBSTRATE 2


Mass: 48419.836 Da / Num. of mol.: 4 / Mutation: D82A,K83A,E172A,N173A,K239A,E359A,K362A,D363A
Source method: isolated from a genetically manipulated source
Details: The fused Maltose binding protein is derived from Escherichia coli O157:H7
Source: (gene. exp.) Serratia sp. (strain FS14) (bacteria), (gene. exp.) Arabidopsis thaliana (thale cress)
Strain: FS14 / Gene: malE, JW3994, BZR1, BIS2, At1g75080, F9E10_7 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A4P1LXE0, UniProt: Q8S307
#2: DNA chain
DNA (5'-D(*TP*TP*GP*AP*CP*AP*CP*GP*TP*GP*TP*CP*AP*AP*A)-3')


Mass: 4593.011 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#3: Polysaccharide
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 299 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.52 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop
Details: 50 mM sodium cacodylate pH 6.5, 200 mM ammonium acetate and 10 mM calcium chloride and 10% (w/v) polyethylene glycol (PEG) 4000

-
Data collection

DiffractionMean temperature: 95 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NE3A / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Dec 19, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.11→47.5 Å / Num. obs: 116947 / % possible obs: 98.1 % / Redundancy: 3.5 % / Biso Wilson estimate: 34.72 Å2 / CC1/2: 0.999 / Net I/σ(I): 12.3
Reflection shellResolution: 2.11→2.15 Å / Mean I/σ(I) obs: 2.1 / Num. unique obs: 5754 / CC1/2: 0.79

-
Processing

Software
NameVersionClassification
PHENIX1.18_3855refinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5ZD4
Resolution: 2.11→36.8 Å / SU ML: 0.2578 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.1
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2438 5846 5.01 %
Rwork0.2065 110949 -
obs0.2083 116795 97.75 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 48.18 Å2
Refinement stepCycle: LAST / Resolution: 2.11→36.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13592 1220 140 299 15251
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00715408
X-RAY DIFFRACTIONf_angle_d0.813821140
X-RAY DIFFRACTIONf_chiral_restr0.05272306
X-RAY DIFFRACTIONf_plane_restr0.00482526
X-RAY DIFFRACTIONf_dihedral_angle_d24.38815760
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.11-2.130.34871890.29083671X-RAY DIFFRACTION97.87
2.13-2.160.31121850.26973712X-RAY DIFFRACTION98.04
2.16-2.190.30762210.2623683X-RAY DIFFRACTION98.09
2.19-2.210.28961920.25583674X-RAY DIFFRACTION97.87
2.21-2.240.29061920.2543679X-RAY DIFFRACTION98.17
2.24-2.270.28722020.25373725X-RAY DIFFRACTION98.13
2.27-2.310.29491920.24933658X-RAY DIFFRACTION98.04
2.31-2.340.32751860.25593748X-RAY DIFFRACTION98.25
2.34-2.380.31122000.25283666X-RAY DIFFRACTION98.32
2.38-2.420.29181970.24753709X-RAY DIFFRACTION98.29
2.42-2.460.29481930.24873698X-RAY DIFFRACTION98.33
2.46-2.50.31151960.24633749X-RAY DIFFRACTION98.55
2.5-2.550.30282000.24053710X-RAY DIFFRACTION98.56
2.55-2.60.24461780.23563709X-RAY DIFFRACTION98.48
2.6-2.660.26721920.23283739X-RAY DIFFRACTION98.47
2.66-2.720.27052140.23043679X-RAY DIFFRACTION98.56
2.72-2.790.29321940.2393729X-RAY DIFFRACTION98.44
2.79-2.860.29881920.25463738X-RAY DIFFRACTION98.5
2.86-2.950.31452110.25543678X-RAY DIFFRACTION98.13
2.95-3.040.2971960.24513702X-RAY DIFFRACTION97.92
3.04-3.150.2421840.22733730X-RAY DIFFRACTION98.47
3.15-3.280.24451780.2213706X-RAY DIFFRACTION97.76
3.28-3.430.23991970.21273691X-RAY DIFFRACTION97.15
3.43-3.610.23081860.20243674X-RAY DIFFRACTION96.94
3.61-3.830.23422210.18743642X-RAY DIFFRACTION96.62
3.83-4.130.21521640.16773688X-RAY DIFFRACTION96.37
4.13-4.540.15921860.15763698X-RAY DIFFRACTION97.17
4.54-5.20.16752180.15123681X-RAY DIFFRACTION96.61
5.2-6.540.2072040.17893682X-RAY DIFFRACTION96.14
6.54-36.80.2181860.15113701X-RAY DIFFRACTION94.55
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.75441232423-0.3555981289-0.8057648069961.8607156211-0.004614586343761.996281449460.04674659458-0.1629550955460.1040684489350.0175897065142-0.0232947583099-0.0426662933902-0.1551946340860.112745774364-0.01610129171820.264910464501-0.032661110670.02712786082680.2069159699640.02716293757770.177931371236-2.6502015414.392106607511.241012434
22.51439038098-1.20867441370.8237060067483.84064142927-0.9109782776112.743455078560.252874738767-0.229954772376-0.45542125520.2678810831570.0529539148922-0.1221354675980.838347583329-0.059962361283-0.2459337268720.491906246486-0.0678020739569-0.1083999553140.2038417822450.005291861482880.35729155893-6.6357851279-36.7537513728.2901646836
32.510624383160.7551419950930.3375980115261.822952625520.06236464599831.73623333885-0.07727915124380.0614739820275-0.06003990204320.3959873112090.164352576938-0.284407577673-0.1038415578440.20721151152-0.08454614607040.4098286482560.102201472329-0.04801588402610.338466351691-0.06341225999180.269859314127-8.0745579606414.34187485744.7923443019
41.580799369261.344447227450.4221217382412.609865397570.6677002197452.395848209850.2044710037030.116477513091-0.3481941263540.07561939800570.0676427131136-0.1397875303630.950248310823-0.184661265776-0.222730167710.494347259331-0.0406189666764-0.1050868242770.2085054774350.02588732651310.401352675473-2.47553105636-36.811535884526.002138742
50.5424748058330.01138258378291.14313900821.93017716593-0.8678620566188.316433838770.205456933908-0.0904478369159-0.08340797352220.368542657120.0370353466760.017926395740.240515391188-0.67696211994-0.2135149526980.234219783269-0.0614101237447-0.001106740395960.2109162850470.01353805599250.223269007694-6.19913129989-23.79503652928.7497379438
61.489335539960.4269083295360.531698559741.19288337018-0.2596609752286.927123296420.0889105277762-0.0712617255971-0.1760552254030.1042517987570.0824295434036-0.1642050341760.2751704970950.276380884812-0.183001600980.259156814889-0.0294288327684-0.005651055389730.156409299583-0.01640554171940.231686642979-3.24682415663-23.792184131725.5843208158
76.144948295753.801135034861.130939148875.699637014722.085415013223.8935044824-0.1314104656420.7088139098730.340899549882-0.5709308593640.1187626084440.228271250772-0.219110548580.2816222554650.02077921128180.2227798162030.06285459869960.003621891204050.3498832166250.0392089245750.20935195320825.85534199-11.478080012335.2454556615
84.00673856770.260915639306-0.2388346252880.972733426429-0.1294065794251.266912152760.10396737785-0.2700516288890.04959715587020.0771923168998-0.127874440249-0.143980886750.00628320194940.523535049660.02342904697030.2627837914510.0122670330805-0.009170326702930.4032216251660.021148924890.17162129326443.2637873656-14.028589020946.2889530577
91.27467626002-2.118290707740.7656278578087.67349152854-5.908376721165.30105799601-0.03588124234330.112278744083-0.0419900418845-0.07588536456930.21364980080.273827670953-0.460942919517-0.702263839024-0.1479530196060.777273833884-0.0911372694219-0.1283285462440.622445587739-0.1582610661990.41944285057245.62453743529.71288242929.9801802907
103.3828138683-0.162651529562-0.3384801406011.38182700681-0.3386345624882.609826932240.04441187264120.08577241453550.0515631944949-0.06039894139260.02299595421210.1985641272410.0697735030658-0.821797120584-0.05695741598650.227918768504-0.0533125660016-0.00245679339930.4250302497020.0180119150970.19055731207852.4039236947-14.496584362411.1134261749
110.7665740593980.34715743455-0.5641361882343.39244533492.004344898452.03055084411-0.0571611612928-0.202336844744-0.190361313060.6628178808340.336526003197-0.290047223805-0.006812784652410.498982886478-0.2002436265910.9163869974910.0409732250043-0.1746315719020.6744377495720.05699399406280.58864103329948.472587585234.236760478828.1149669285
120.152070045055-0.516226801511-0.9888156861331.433756092283.296638137887.513942439310.3286277077750.1901730432150.003472032569710.2623068053010.0197359040755-0.05877834982671.69605509047-0.119242994628-0.3088852251660.8997068189750.0120552633034-0.08146705066071.01606408480.0008018328807580.38189695169346.798924276523.773023243929.6082533795
130.3924420945920.583687702335-1.834932164150.769873434026-2.857075859362.038288615180.187875668703-0.13778759043-0.00508102949235-0.2875738146110.1120550961820.157617493541.864607498960.0853728542303-0.2640106315921.01085125840.149125813308-0.1024828305831.049675596110.01920133310250.3602829047345.181506882323.737868531226.0003896631
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'C' and (resid -348 through 26 )CA-348 - 261 - 375
22chain 'C' and (resid 27 through 88 )CA27 - 88376 - 437
33chain 'D' and (resid -347 through 26 )DC-347 - 261 - 374
44chain 'D' and (resid 27 through 88 )DC27 - 88375 - 436
55chain 'G' and (resid -3 through 11 )GE-3 - 11
66chain 'H' and (resid -3 through 11 )HF-3 - 11
77chain 'A' and (resid -348 through -276 )AG-348 - -2761 - 73
88chain 'A' and (resid -275 through 3 )AG-275 - 374 - 352
99chain 'A' and (resid 4 through 88 )AG4 - 88353 - 437
1010chain 'B' and (resid -346 through 20 )BI-346 - 202 - 368
1111chain 'B' and (resid 21 through 88 )BI21 - 88369 - 436
1212chain 'E' and (resid -3 through 11 )EK-3 - 11
1313chain 'F' and (resid -3 through 11 )FL-3 - 11

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more