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- PDB-1e9y: Crystal structure of Helicobacter pylori urease in complex with a... -

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Basic information

Entry
Database: PDB / ID: 1e9y
TitleCrystal structure of Helicobacter pylori urease in complex with acetohydroxamic acid
Components
  • UREASE SUBUNIT ALPHA
  • UREASE SUBUNIT BETA
KeywordsHYDROLASE / DODECAMER
Function / homology
Function and homology information


urease complex / urease / urease activity / urea catabolic process / nickel cation binding / cytoplasm
Similarity search - Function
Urease, gamma-beta subunit / Urease, subunit B / Urease, beta subunit / Urease; subunit A / Urease, gamma-like subunit / Urease active site / Urease active site. / Urease nickel binding site / Urease nickel ligands signature. / Urease, beta subunit ...Urease, gamma-beta subunit / Urease, subunit B / Urease, beta subunit / Urease; subunit A / Urease, gamma-like subunit / Urease active site / Urease active site. / Urease nickel binding site / Urease nickel ligands signature. / Urease, beta subunit / Urease, alpha subunit / Urease alpha subunit, C-terminal / Urease, beta subunit superfamily / Urease beta subunit / Urease domain profile. / Urease alpha-subunit, N-terminal domain / Urease alpha-subunit, N-terminal domain / Urease, gamma/gamma-beta subunit / Urease, gamma subunit superfamily / Urease, gamma subunit / Urease, subunit C; domain 1 / Urease, subunit C, domain 1 / Amidohydrolase family / Metal-dependent hydrolase, composite domain superfamily / Amidohydrolase-related / Metal-dependent hydrolases / Metal-dependent hydrolase / Ribbon / Roll / TIM Barrel / Alpha-Beta Barrel / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ACETOHYDROXAMIC ACID / NICKEL (II) ION / Urease subunit alpha / Urease subunit beta
Similarity search - Component
Biological speciesHELICOBACTER PYLORI (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsHa, N.-C. / Oh, S.-T. / Oh, B.-H.
CitationJournal: Nat.Struct.Biol. / Year: 2001
Title: Supramolecular Assembly and Acid Resistance of Helicobacter Pylori Urease
Authors: Ha, N.-C. / Oh, S.-T. / Sung, J.Y. / Cha, K.-A. / Hyung Lee, M. / Oh, B.-H.
History
DepositionNov 1, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 1, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UREASE SUBUNIT ALPHA
B: UREASE SUBUNIT BETA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,5265
Polymers88,3332
Non-polymers1923
Water1,18966
1
A: UREASE SUBUNIT ALPHA
B: UREASE SUBUNIT BETA
hetero molecules
x 12


Theoretical massNumber of molelcules
Total (without water)1,062,30760
Polymers1,059,99724
Non-polymers2,30936
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_566z,-x+1,-y+11
crystal symmetry operation7_665-z+1,-x+1,y1
crystal symmetry operation10_656-y+1,z,-x+11
crystal symmetry operation5_555z,x,y1
crystal symmetry operation12_665-y+1,-z+1,x1
crystal symmetry operation11_566y,-z+1,-x+11
crystal symmetry operation4_566x,-y+1,-z+11
crystal symmetry operation8_656-z+1,x,-y+11
crystal symmetry operation3_656-x+1,y,-z+11
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation9_555y,z,x1
Buried area207540 Å2
ΔGint-1220.2 kcal/mol
Surface area245140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)178.160, 178.160, 178.160
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number197
Space group name H-MI23

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Components

#1: Protein UREASE SUBUNIT ALPHA / / UREA AMIDOHYDROLASE SUBUNIT ALPHA


Mass: 26571.662 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HELICOBACTER PYLORI (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P14916, urease
#2: Protein UREASE SUBUNIT BETA / / UREA AMIDOHYDROLASE SUBUNIT BETA


Mass: 61761.445 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HELICOBACTER PYLORI (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P69996, urease
#3: Chemical ChemComp-HAE / ACETOHYDROXAMIC ACID / Acetohydroxamic acid


Mass: 75.067 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H5NO2 / Comment: inhibitor, medication*YM
#4: Chemical ChemComp-NI / NICKEL (II) ION / Nickel


Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 66 / Source method: isolated from a natural source / Formula: H2O
Compound detailsHYDROLYSES UREA INTO CO(2) AND 2 NH(3).

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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: 2.67 Å3/Da / Density % sol: 51 %
Crystal growpH: 6.5 / Details: pH 6.50
Crystal grow
*PLUS
Temperature: 12 ℃ / Method: vapor diffusion, hanging drop / Details: used macroseeding
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 mg/mlprotein1drop
20.1 MMES1reservoir
325 %(v/v)Jeffamine-M6001reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→20 Å / Num. obs: 22236 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 14 % / Rsym value: 0.079
Reflection
*PLUS
Highest resolution: 2.8 Å / Lowest resolution: 20 Å / Num. obs: 23322 / % possible obs: 100 % / Num. measured all: 330949 / Rmerge(I) obs: 0.079
Reflection shell
*PLUS
% possible obs: 100 % / Rmerge(I) obs: 0.323

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Processing

Software
NameClassification
CNSrefinement
DPSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→20 Å / Cross valid method: THROUGHOUT / σ(F): 1
RfactorNum. reflection% reflection
Rfree0.282 -5 %
Rwork0.213 --
obs0.213 21534 92.5 %
Refinement stepCycle: LAST / Resolution: 3→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6199 0 7 66 6272
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.0078
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.27
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
Software
*PLUS
Name: CNS / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.8 Å / Lowest resolution: 40 Å / σ(F): 1 / Rfactor Rfree: 0.279
Solvent computation
*PLUS
Displacement parameters
*PLUS

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