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- PDB-6g3g: Crystal structure of EDDS lyase in complex with succinate -

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Basic information

Entry
Database: PDB / ID: 6g3g
TitleCrystal structure of EDDS lyase in complex with succinate
ComponentsArgininosuccinate lyase
KeywordsLYASE / C-N Lyase / metal chelator / EDDS / tetramer / succinate / aspartase fumarase superfamily
Function / homology
Function and homology information


argininosuccinate lyase / argininosuccinate lyase activity / arginine biosynthetic process via ornithine
Similarity search - Function
Argininosuccinate lyase / Argininosuccinate lyase, C-terminal / Argininosuccinate lyase C-terminal / Fumarate lyase family / Fumarate lyase, N-terminal / Lyase / Fumarase/histidase, N-terminal / L-Aspartase-like
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / SUCCINIC ACID / argininosuccinate lyase
Similarity search - Component
Biological speciesChelativorans sp.
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.606 Å
AuthorsPoddar, H. / Thunnissem, A.M.W.H. / Poelarends, G.J.
Funding support Netherlands, 1items
OrganizationGrant numberCountry
European Research Council242293 Netherlands
CitationJournal: Biochemistry / Year: 2018
Title: Structural Basis for the Catalytic Mechanism of Ethylenediamine- N, N'-disuccinic Acid Lyase, a Carbon-Nitrogen Bond-Forming Enzyme with a Broad Substrate Scope.
Authors: Poddar, H. / de Villiers, J. / Zhang, J. / Puthan Veetil, V. / Raj, H. / Thunnissen, A.W.H. / Poelarends, G.J.
History
DepositionMar 25, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 16, 2018Provider: repository / Type: Initial release
Revision 1.1May 23, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI ..._citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2May 30, 2018Group: Data collection / Database references / Category: citation / Item: _citation.title
Revision 1.3Jul 11, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Argininosuccinate lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,72510
Polymers55,7581
Non-polymers9679
Water2,054114
1
A: Argininosuccinate lyase
hetero molecules

A: Argininosuccinate lyase
hetero molecules

A: Argininosuccinate lyase
hetero molecules

A: Argininosuccinate lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)226,90140
Polymers223,0334
Non-polymers3,86836
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
crystal symmetry operation3_556-x,y,-z+11
crystal symmetry operation4_556x,-y,-z+11
Buried area43100 Å2
ΔGint-8 kcal/mol
Surface area58900 Å2
MethodPISA
Unit cell
Length a, b, c (Å)145.072, 145.954, 151.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number22
Space group name H-MF222
Components on special symmetry positions
IDModelComponents
11A-811-

HOH

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Components

#1: Protein Argininosuccinate lyase /


Mass: 55758.246 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chelativorans sp. (strain BNC1) (bacteria)
Strain: BNC1 / Gene: Meso_0564 / Plasmid: pBADN / Production host: Escherichia coli (E. coli) / References: UniProt: Q11KV9
#2: Chemical ChemComp-SIN / SUCCINIC ACID / Succinic acid


Mass: 118.088 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H6O4
#3: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C4H10O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 114 / 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: 3.59 Å3/Da / Density % sol: 65.7 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M Sodium cacodylate pH 6.5, 0.2 - 0.3 M sodium succinate

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.54 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 12, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.6→52.5 Å / Num. obs: 24456 / % possible obs: 99.5 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 28.5
Reflection shellResolution: 2.6→2.71 Å

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6G3D

6g3d


Resolution: 2.606→51.446 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 21.46
RfactorNum. reflection% reflection
Rfree0.2234 1235 5.05 %
Rwork0.1903 --
obs0.1919 24456 99.38 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.606→51.446 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3812 0 64 114 3990
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0033929
X-RAY DIFFRACTIONf_angle_d0.5915305
X-RAY DIFFRACTIONf_dihedral_angle_d14.1212381
X-RAY DIFFRACTIONf_chiral_restr0.037612
X-RAY DIFFRACTIONf_plane_restr0.004685
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6063-2.71070.28341390.22152450X-RAY DIFFRACTION96
2.7107-2.8340.26061400.22582559X-RAY DIFFRACTION100
2.834-2.98340.26021290.23632574X-RAY DIFFRACTION100
2.9834-3.17030.26751470.2212569X-RAY DIFFRACTION100
3.1703-3.41510.25761440.21942559X-RAY DIFFRACTION100
3.4151-3.75860.23851280.19452608X-RAY DIFFRACTION100
3.7586-4.30230.21391400.16792591X-RAY DIFFRACTION100
4.3023-5.41950.16641350.14492634X-RAY DIFFRACTION100
5.4195-51.45590.17431330.17532677X-RAY DIFFRACTION99

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