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- PDB-6jao: Crystal structure of ABC transporter alpha-glycoside-binding muta... -

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Basic information

Entry
Database: PDB / ID: 6jao
TitleCrystal structure of ABC transporter alpha-glycoside-binding mutant protein R356A in complex with palatinose
ComponentsABC transporter, periplasmic substrate-binding proteinATP-binding cassette transporter
KeywordsSUGAR BINDING PROTEIN / Carbohydrate-bindingsite / alpha-glycoside-binding protein / Ligand selection / Multi-substrate transporter / Sugar replacement / Venus Fly-trap mechanism
Function / homologyBacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Periplasmic binding protein-like II / D-Maltodextrin-Binding Protein; domain 2 / 3-Layer(aba) Sandwich / Alpha Beta / ACETATE ION / CITRIC ACID / ABC transporter, periplasmic substrate-binding protein
Function and homology information
Biological speciesThermus thermophilus (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.77 Å
AuthorsKanaujia, S.P. / Chandravanshi, M. / Gogoi, P.
Funding support India, 1items
OrganizationGrant numberCountry
Department of Biotechnology (India)BT/563/NE/U-Excel/2016 India
CitationJournal: Febs J. / Year: 2020
Title: Structural and thermodynamic correlation illuminates the selective transport mechanism of disaccharide alpha-glycosides through ABC transporter.
Authors: Chandravanshi, M. / Gogoi, P. / Kanaujia, S.P.
History
DepositionJan 24, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 30, 2019Provider: repository / Type: Initial release
Revision 1.1May 6, 2020Group: Data collection / Database references / Category: chem_comp / citation
Item: _chem_comp.type / _citation.journal_volume ..._chem_comp.type / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ABC transporter, periplasmic substrate-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,7966
Polymers46,0821
Non-polymers7155
Water10,034557
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area590 Å2
ΔGint4 kcal/mol
Surface area16270 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.420, 85.420, 146.150
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-668-

HOH

21A-985-

HOH

31A-1154-

HOH

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Components

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Protein / Sugars , 2 types, 2 molecules A

#1: Protein ABC transporter, periplasmic substrate-binding protein / ATP-binding cassette transporter / alpha-GlyBP


Mass: 46081.883 Da / Num. of mol.: 1 / Mutation: R356A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (bacteria)
Strain: HB8 / ATCC 27634 / DSM 579 / Gene: TTHA0356 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) / References: UniProt: Q5SLD7
#2: Polysaccharide alpha-D-glucopyranose-(1-6)-alpha-D-fructofuranose


Type: oligosaccharide / Mass: 342.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpa1-6DFrufa2-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2a_2-5][a2122h-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[][a-D-Fruf]{[(6+1)][a-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 4 types, 561 molecules

#3: Chemical ChemComp-CIT / CITRIC ACID / Citric acid


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 557 / Source method: isolated from a natural source / Formula: H2O

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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: 2.92 Å3/Da / Density % sol: 57.93 % / Description: Tetragonal
Crystal growTemperature: 277 K / Method: microbatch / pH: 5
Details: 0.05 M Citric Acid, 0.05 M Bis-Tris Propane, 16% PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Feb 26, 2018 / Details: VariMax HF
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.77→73.75 Å / Num. obs: 53234 / % possible obs: 100 % / Redundancy: 17.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.08 / Rpim(I) all: 0.027 / Rrim(I) all: 0.085 / Net I/σ(I): 24
Reflection shellResolution: 1.77→9.04 Å / Redundancy: 16.1 % / Rmerge(I) obs: 0.302 / Mean I/σ(I) obs: 6.1 / Num. unique obs: 2987 / CC1/2: 0.982 / Rpim(I) all: 0.111 / Rrim(I) all: 0.322 / % possible all: 100

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation6.48 Å55.82 Å
Translation6.48 Å55.82 Å

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Processing

Software
NameVersionClassification
HKL-30003000data collection
iMOSFLM7.2.2data reduction
Aimless0.7.3data scaling
PHASER2.8.2phasing
REFMAC5.8.0238refinement
Coot0.8.9.1model building
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6J9W

6j9w


Resolution: 1.77→73.75 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.943 / SU B: 1.882 / SU ML: 0.059 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.093 / ESU R Free: 0.1
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1994 2607 4.9 %RANDOM
Rwork0.1549 ---
obs0.157 50374 99.62 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 81.54 Å2 / Biso mean: 20.911 Å2 / Biso min: 9.81 Å2
Baniso -1Baniso -2Baniso -3
1-0.21 Å2-0 Å2-0 Å2
2--0.21 Å2-0 Å2
3----0.43 Å2
Refinement stepCycle: final / Resolution: 1.77→73.75 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3221 0 48 557 3826
Biso mean--25.63 34.37 -
Num. residues----404
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0193414
X-RAY DIFFRACTIONr_bond_other_d0.0010.023111
X-RAY DIFFRACTIONr_angle_refined_deg1.8271.9544655
X-RAY DIFFRACTIONr_angle_other_deg0.92537185
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8955421
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.92522.588170
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.76215540
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.7771537
X-RAY DIFFRACTIONr_chiral_restr0.1140.2488
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.0213851
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02766
LS refinement shellResolution: 1.773→1.819 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.214 184 -
Rwork0.155 3691 -
all-3875 -
obs--99.92 %

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