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- PDB-2qet: Structure of the mutant S211A of the ribosome inactivating protei... -

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Basic information

Entry
Database: PDB / ID: 2qet
TitleStructure of the mutant S211A of the ribosome inactivating protein PDL4 from P. dioica in complex with adenine
ComponentsRibosome-inactivating protein PD-L4
KeywordsHYDROLASE / crystal / ribosome inactivating protein
Function / homology
Function and homology information


rRNA N-glycosylase / rRNA N-glycosylase activity / defense response / toxin activity / negative regulation of translation
Similarity search - Function
Ricin (A Subunit), domain 2 / Ricin (A Subunit), domain 2 / Ricin (A subunit); domain 1 / Ricin (A subunit), domain 1 / Ribosome-inactivating protein conserved site / Shiga/ricin ribosomal inactivating toxins active site signature. / Ribosome-inactivating protein type 1/2 / Ribosome-inactivating protein / Ribosome-inactivating protein, subdomain 1 / Ribosome-inactivating protein, subdomain 2 ...Ricin (A Subunit), domain 2 / Ricin (A Subunit), domain 2 / Ricin (A subunit); domain 1 / Ricin (A subunit), domain 1 / Ribosome-inactivating protein conserved site / Shiga/ricin ribosomal inactivating toxins active site signature. / Ribosome-inactivating protein type 1/2 / Ribosome-inactivating protein / Ribosome-inactivating protein, subdomain 1 / Ribosome-inactivating protein, subdomain 2 / Ribosome-inactivating protein superfamily / Ribosome inactivating protein / Few Secondary Structures / Irregular / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENINE / Ribosome-inactivating protein PD-L3/PD-L4
Similarity search - Component
Biological speciesPhytolacca dioica (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.24 Å
AuthorsRuggiero, A. / Berisio, R.
CitationJournal: Proteins / Year: 2008
Title: Atomic resolution (1.1 A) structure of the ribosome-inactivating protein PD-L4 from Phytolacca dioica L. leaves
Authors: Ruggiero, A. / Chambery, A. / Di Maro, A. / Parente, A. / Berisio, R.
History
DepositionJun 26, 2007Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 26, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 10, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / diffrn_source ...database_2 / diffrn_source / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Ribosome-inactivating protein PD-L4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,3402
Polymers29,2051
Non-polymers1351
Water8,845491
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)43.619, 61.541, 91.626
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Ribosome-inactivating protein PD-L4 / rRNA N- glycosidase PD-L3/PD-L4


Mass: 29205.115 Da / Num. of mol.: 1 / Mutation: S211A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Phytolacca dioica (plant) / Plasmid: pET22b(+) / Production host: Escherichia coli (E. coli) / References: UniProt: P84854, rRNA N-glycosylase
#2: Chemical ChemComp-ADE / ADENINE


Mass: 135.127 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H5N5
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 491 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.1 Å3/Da / Density % sol: 41.56 %
Crystal growMethod: vapor diffusion / Details: VAPOR DIFFUSION

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Apr 8, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 1.24→30 Å / Num. all: 75869 / Num. obs: 68965
Reflection shellHighest resolution: 1.24 Å

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Processing

Software
NameClassification
HKL-2000data collection
IlMilionemodel building
SHELXL-97refinement
HKL-2000data reduction
HKL-2000data scaling
IlMilionephasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1qcg

1qcg


Resolution: 1.24→10 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.155 -random
Rwork0.122 --
all-65300 -
obs-65300 -
Refinement stepCycle: LAST / Resolution: 1.24→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2092 0 10 491 2593
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.029
X-RAY DIFFRACTIONs_angle_d0.037

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