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- PDB-6h91: Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in... -

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Basic information

Entry
Database: PDB / ID: 6h91
TitlePhosphorylated beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.4 A
ComponentsBeta-phosphoglucomutase
KeywordsISOMERASE / phosphoglucomutase / phospho-enzyme / acetylphosphate
Function / homology
Function and homology information


beta-phosphoglucomutase / beta-phosphoglucomutase activity / carbohydrate metabolic process / magnesium ion binding / cytoplasm
Similarity search - Function
Beta-phosphoglucomutase / Beta-phosphoglucomutase hydrolase / : / Phosphoglycolate phosphatase-like, domain 2 / HAD hydrolase, subfamily IA / haloacid dehalogenase-like hydrolase / HAD superfamily / HAD-like superfamily
Similarity search - Domain/homology
ACETYLPHOSPHATE / Beta-phosphoglucomutase
Similarity search - Component
Biological speciesLactococcus lactis subsp. lactis Il1403 (lactic acid bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å
AuthorsRobertson, A.J. / Bisson, C. / Waltho, J.P.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research CouncilBB/M021637/1 United Kingdom
Biotechnology and Biological Sciences Research CouncilBB/K016245/1 United Kingdom
CitationJournal: To Be Published
Title: Transition state of phospho-enzyme hydrolysis in beta-phosphoglucomutase
Authors: Robertson, A.J. / Bisson, C. / Waltho, J.P.
History
DepositionAug 3, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 26, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 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

Downloads & links

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Assembly

Deposited unit
A: Beta-phosphoglucomutase
B: Beta-phosphoglucomutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,0307
Polymers48,6392
Non-polymers3915
Water2,018112
1
A: Beta-phosphoglucomutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,4843
Polymers24,3201
Non-polymers1642
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Beta-phosphoglucomutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,5464
Polymers24,3201
Non-polymers2263
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)38.330, 117.230, 52.930
Angle α, β, γ (deg.)90.00, 97.75, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Beta-phosphoglucomutase / Beta-PGM


Mass: 24319.574 Da / Num. of mol.: 2 / Mutation: K125R, Y206H
Source method: isolated from a genetically manipulated source
Details: Residue D8 is modified by phosphorylation in the pre-formed crystal.
Source: (gene. exp.) Lactococcus lactis subsp. lactis Il1403 (lactic acid bacteria)
Gene: pgmB, LL0429, L0001 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P71447, beta-phosphoglucomutase
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: Mg
#3: Chemical ChemComp-UVW / ACETYLPHOSPHATE


Mass: 140.032 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H5O5P / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 112 / 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: 2.42 Å3/Da / Density % sol: 49.23 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 24-34% PEG 4000, 200 mM sodium acetate, 50 mM TRIS pH 7.5, The crystal was cryoprotected in its original mother liquor plus an additional 25% ethylene glycol and 30mM acetylphosphate.
PH range: 7.2 / Temp details: 100

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97779 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 23, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97779 Å / Relative weight: 1
ReflectionResolution: 2.38→58.62 Å / Num. obs: 18430 / % possible obs: 99 % / Redundancy: 3.7 % / CC1/2: 0.987 / Rmerge(I) obs: 0.12 / Rpim(I) all: 0.084 / Rrim(I) all: 0.165 / Net I/σ(I): 6.7
Reflection shellResolution: 2.38→2.44 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.597 / Num. unique obs: 1355 / CC1/2: 0.526 / Rpim(I) all: 0.438 / Rrim(I) all: 0.813 / % possible all: 98.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
xia2data reduction
xia2data scaling
Coot0.8.7model building
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2WHE

2whe


Resolution: 2.38→58.62 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.875 / SU B: 13.495 / SU ML: 0.303 / Cross valid method: THROUGHOUT / ESU R: 0.537 / ESU R Free: 0.325 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.29875 945 5.1 %RANDOM
Rwork0.2188 ---
obs0.22299 17460 99.01 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.3 Å2
Baniso -1Baniso -2Baniso -3
1-0.47 Å20 Å20.01 Å2
2---0.24 Å2-0 Å2
3----0.22 Å2
Refinement stepCycle: 1 / Resolution: 2.38→58.62 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3368 0 22 112 3502
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0193445
X-RAY DIFFRACTIONr_bond_other_d0.0010.023279
X-RAY DIFFRACTIONr_angle_refined_deg1.5391.9864664
X-RAY DIFFRACTIONr_angle_other_deg0.96737623
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5885434
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.52525.6150
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.43815600
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.5161514
X-RAY DIFFRACTIONr_chiral_restr0.0790.2526
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213810
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02636
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.1833.9481742
X-RAY DIFFRACTIONr_mcbond_other2.1823.9481741
X-RAY DIFFRACTIONr_mcangle_it3.385.9182174
X-RAY DIFFRACTIONr_mcangle_other3.3795.9192175
X-RAY DIFFRACTIONr_scbond_it2.3454.211703
X-RAY DIFFRACTIONr_scbond_other2.3454.2111704
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.786.192491
X-RAY DIFFRACTIONr_long_range_B_refined5.73546.8263769
X-RAY DIFFRACTIONr_long_range_B_other5.7446.8343769
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.38→2.442 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.414 56 -
Rwork0.301 1296 -
obs--98.76 %

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