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- PDB-3lcf: The D-sialic acid aldolase mutant V251I -

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Basic information

Entry
Database: PDB / ID: 3lcf
TitleThe D-sialic acid aldolase mutant V251I
ComponentsN-acetylneuraminate lyase
KeywordsLYASE / Tim barrel / Carbohydrate metabolism / Schiff base
Function / homology
Function and homology information


N-acetylneuraminate lyase / N-acetylneuraminate lyase activity / N-acetylneuraminate catabolic process / single-species biofilm formation / carbohydrate metabolic process / identical protein binding / cytosol
Similarity search - Function
N-acetylneuraminate lyase / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase class I / Aldolase-type TIM barrel ...N-acetylneuraminate lyase / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
N-acetylneuraminate lyase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.86 Å
AuthorsChou, C.-Y. / Wang, A.H.-J. / Ko, T.-P.
CitationJournal: To be Published
Title: Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val251
Authors: Chou, C.-Y. / Ko, T.-P. / Wu, K.-J. / Huang, K.-F. / Lin, C.-H. / Wong, C.-H. / Wang, A.H.-J.
History
DepositionJan 11, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jan 19, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: N-acetylneuraminate lyase
B: N-acetylneuraminate lyase
C: N-acetylneuraminate lyase
D: N-acetylneuraminate lyase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,6068
Polymers141,2214
Non-polymers3844
Water23,3831298
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8680 Å2
ΔGint-57 kcal/mol
Surface area41390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.082, 121.082, 197.098
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein
N-acetylneuraminate lyase / N-acetylneuraminic acid aldolase / N-acetylneuraminate pyruvate-lyase / Sialic acid lyase / Sialate ...N-acetylneuraminic acid aldolase / N-acetylneuraminate pyruvate-lyase / Sialic acid lyase / Sialate lyase / Sialic acid aldolase / NALase


Mass: 35305.316 Da / Num. of mol.: 4 / Mutation: V251I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b3225, JW3194, nanA, npl / Plasmid: pET16b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0A6L4, N-acetylneuraminate lyase
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1298 / 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: 2.95 Å3/Da / Density % sol: 58.35 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 2.0M ammonium sulfate, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 0.97622 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Apr 23, 2009 / Details: vertically focusing mirror
RadiationMonochromator: horizontally focusing single crystal Si(111) bent Monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97622 Å / Relative weight: 1
ReflectionResolution: 1.86→30 Å / Num. all: 140492 / Num. obs: 139509 / % possible obs: 99.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 6.3 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 35.3
Reflection shellResolution: 1.86→1.93 Å / Redundancy: 6 % / Rmerge(I) obs: 0.427 / Mean I/σ(I) obs: 3.8 / Num. unique all: 13089 / % possible all: 94.3

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Processing

Software
NameClassification
Blu-Icedata collection
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB enrty 1NAL

1nal


Resolution: 1.86→27.95 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2129 6732 -RANDOM
Rwork0.18 ---
all0.181645 132700 --
obs0.181645 125968 89.7 %-
Solvent computationBsol: 65.084 Å2
Displacement parametersBiso max: 72.25 Å2 / Biso mean: 26.236 Å2 / Biso min: 13.01 Å2
Baniso -1Baniso -2Baniso -3
1-0.935 Å2-0.005 Å20 Å2
2--0.935 Å20 Å2
3----1.87 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.23 Å0.19 Å
Luzzati d res low-5 Å
Luzzati sigma a0.15 Å0.13 Å
Refinement stepCycle: LAST / Resolution: 1.86→27.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9111 0 20 1298 10429
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_angle_deg1.26795
X-RAY DIFFRACTIONc_bond_d0.005005
X-RAY DIFFRACTIONc_mcbond_it1.0951.5
X-RAY DIFFRACTIONc_scbond_it1.8642
X-RAY DIFFRACTIONc_mcangle_it1.5752
X-RAY DIFFRACTIONc_scangle_it2.7562.5
LS refinement shellResolution: 1.86→1.93 Å / Rfactor Rfree error: 0.0317
RfactorNum. reflection% reflection
Rfree0.2662 608 -
Rwork0.2345 --
obs-11483 87.73 %
Xplor file
Refine-IDSerial noParam file
X-RAY DIFFRACTION1CNS_TOPPAR:protein_rep.param
X-RAY DIFFRACTION2CNS_TOPPAR:water_rep.param
X-RAY DIFFRACTION3CNS_TOPPAR:ion.param

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