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- PDB-7upv: Structure of maize BZR1-type beta-amylase provides new insights i... -

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Basic information

Entry
Database: PDB / ID: 7upv
TitleStructure of maize BZR1-type beta-amylase provides new insights into its noncatalytic adaptation
ComponentsBeta-amylase
KeywordsHYDROLASE / GH-14 / maize beta-amylase / BZR1-BAM8
Function / homology
Function and homology information


beta-amylase / beta-amylase activity / amylopectin maltohydrolase activity / polysaccharide catabolic process / regulation of gene expression
Similarity search - Function
BES1/BZR1 plant transcription factor, N-terminal / BES1/BZR1 plant transcription factor, N-terminal / Glycoside hydrolase, family 14 / Glycosyl hydrolase family 14 / Glycoside hydrolase superfamily
Similarity search - Domain/homology
Biological speciesZea mays (maize)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.84 Å
AuthorsPalayam, M. / Sun, F. / Shabek, N.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P30 GM124169-01 United States
CitationJournal: J.Struct.Biol. / Year: 2022
Title: Structure of maize BZR1-type beta-amylase BAM8 provides new insights into its noncatalytic adaptation.
Authors: Sun, F. / Palayam, M. / Shabek, N.
History
DepositionApr 18, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 17, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2022Group: Database references / Category: citation
Item: _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Aug 31, 2022Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.3Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Beta-amylase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,5402
Polymers51,4481
Non-polymers921
Water72140
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)50.896, 69.141, 59.123
Angle α, β, γ (deg.)90.000, 95.040, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Beta-amylase


Mass: 51447.871 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zea mays (maize) / Gene: ZEAMMB73_Zm00001d053975 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A1D6QTZ9, beta-amylase
#2: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.01 Å3/Da / Density % sol: 38.93 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 0.2M MgCl2, 0.1M Sodium citrate tribasic dihydrate, 8% Polyethylene glycol 20000
PH range: 5-6

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 12, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 35028 / % possible obs: 98.19 % / Redundancy: 3.2 % / Rsym value: 0.05 / Net I/σ(I): 14.7
Reflection shellResolution: 1.8→1.9 Å / Num. unique obs: 3198 / CC1/2: 0.187

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.27data extraction
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1BYA
Resolution: 1.84→44.83 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.93 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2562 1991 5.71 %
Rwork0.2085 32853 -
obs0.2113 34844 98.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 95.34 Å2 / Biso mean: 27.1083 Å2 / Biso min: 12.1 Å2
Refinement stepCycle: final / Resolution: 1.84→44.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3547 0 6 40 3593
Biso mean--31.39 21.78 -
Num. residues----440
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.84-1.890.36411200.3352006212684
1.89-1.940.36851360.3072233236994
1.94-20.30291410.26552302244398
2-2.060.28991430.25762370251399
2.06-2.130.3161450.2312386253199
2.13-2.220.291450.22223782523100
2.22-2.320.25961440.219523812525100
2.32-2.440.25551430.224523662509100
2.44-2.590.26471460.211824052551100
2.59-2.790.28521430.2323692512100
2.8-3.080.29131450.221723882533100
3.08-3.520.24731450.210424102555100
3.52-4.440.20521460.164124032549100
4.44-44.830.20571490.159924562605100

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