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- PDB-1f7b: CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEM... -

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Basic information

Entry
Database: PDB / ID: 1f7b
TitleCRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II IN COMPLEX WITH 4-OXO-SIALIC ACID
ComponentsN-ACETYL-NEURAMINATE LYASE
KeywordsLYASE / BETA BARREL
Function / homology
Function and homology information


N-acetylneuraminate lyase / N-acetylneuraminate lyase activity / N-acetylneuraminate catabolic process / carbohydrate metabolic process / 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
Chem-NAU / Chem-NAV / N-acetylneuraminate lyase
Similarity search - Component
Biological speciesHaemophilus influenzae (bacteria)
MethodX-RAY DIFFRACTION / Resolution: 1.8 Å
AuthorsBarbosa, J.A.R.G. / Smith, B.J. / DeGori, R. / Lawrence, M.C.
CitationJournal: J.Mol.Biol. / Year: 2000
Title: Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.
Authors: Barbosa, J.A.R.G. / Smith, B.J. / DeGori, R. / Ooi, H.C. / Marcuccio, S.M. / Campi, E.M. / Jackson, W.R. / Brossmer, R. / Sommer, M. / Lawrence, M.C.
History
DepositionJun 26, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 22, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: N-ACETYL-NEURAMINATE LYASE
C: N-ACETYL-NEURAMINATE LYASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,7635
Polymers65,1232
Non-polymers6403
Water14,268792
1
A: N-ACETYL-NEURAMINATE LYASE
C: N-ACETYL-NEURAMINATE LYASE
hetero molecules

A: N-ACETYL-NEURAMINATE LYASE
C: N-ACETYL-NEURAMINATE LYASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,52610
Polymers130,2464
Non-polymers1,2806
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,-y,z1
Buried area12130 Å2
ΔGint-70 kcal/mol
Surface area38980 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)65.625, 117.990, 80.896
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
DetailsThe biological assembly is a tetramer constructed from chains A and C generated by the two-fold.

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Components

#1: Protein N-ACETYL-NEURAMINATE LYASE / NAL


Mass: 32561.570 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Haemophilus influenzae (bacteria) / Plasmid: PKKTAC / Production host: Escherichia coli (E. coli) / References: UniProt: P44539, N-acetylneuraminate lyase
#2: Chemical ChemComp-NAU / 4,4,6,7,8,9-HEXAHYDROXY-5-METHYLCARBOXAMIDONONANOIC ACID


Mass: 311.286 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H21NO9
#3: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-NAV / 6,7,8,9-TETRAHYDROXY-5-METHYLCARBOXAMIDO-4-OXONONANOIC ACID


Mass: 293.270 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H19NO8
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 792 / 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: 2.4 Å3/Da / Density % sol: 48.84 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6
Details: PEG 4000, sodium acetate, ammonium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystal grow
*PLUS
pH: 7.5
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
16 mg/mlprotein1drop
220 mMTris-HCl1drop
390 mM1dropNaCl
419 %(w/v)PEG40001reservoir
50.1 M1reservoirNH4OAc
60.1 M1reservoirNaOAc

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Data collection

DiffractionMean temperature: 113 K
Diffraction sourceSource: ROTATING ANODE / Type: MACSCIENCE / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS II / Detector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.8→15 Å / Num. all: 59168 / Num. obs: 52684 / % possible obs: 89 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 21
Reflection shellResolution: 1.8→1.86 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.2 / Num. unique all: 5816 / % possible all: 42.4
Reflection
*PLUS
Num. measured all: 231047
Reflection shell
*PLUS
% possible obs: 42.4 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 5.2

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Processing

Software
NameClassification
X-PLORmodel building
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing
RefinementResolution: 1.8→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.21 2640 -RANDOM
Rwork0.167 ---
all-52550 --
obs-52550 89 %-
Refinement stepCycle: LAST / Resolution: 1.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4520 0 42 792 5354
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.009
X-RAY DIFFRACTIONo_angle_deg0.026
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
σ(F): 0 / Rfactor obs: 0.167 / Rfactor Rfree: 0.21
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.064

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