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- PDB-4uu4: Crystal structure of LptH, the LptA homologous periplasmic compon... -

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Basic information

Entry
Database: PDB / ID: 4uu4
TitleCrystal structure of LptH, the LptA homologous periplasmic component of the conserved lipopolysaccharide transport device from Pseudomonas aeruginosa
ComponentsPERIPLASMIC LIPOPOLYSACCHARIDE TRANSPORT PROTEIN LPTH
KeywordsTRANSPORT PROTEIN / LPTH / LPTA / LPS
Function / homology
Function and homology information


lipopolysaccharide transport => GO:0015920 / glycolipid transfer activity / lipopolysaccharide transport / Gram-negative-bacterium-type cell outer membrane assembly / lipopolysaccharide binding / cell outer membrane / outer membrane-bounded periplasmic space
Similarity search - Function
Lipopolysaccharide (LPS) transport protein A like domain / Lipopolysaccharide export system protein LptA / lipopolysaccharide transport protein A fold / Organic solvent tolerance-like, N-terminal / LptA/(LptD N-terminal domain) LPS transport protein / Sandwich / Mainly Beta
Similarity search - Domain/homology
Lipopolysaccharide export system protein LptA
Similarity search - Component
Biological speciesPSEUDOMONAS AERUGINOSA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.751 Å
AuthorsBollati, M. / Villa, R. / Gourlay, L.J. / Barbiroli, A. / Deho, G. / Benedet, M. / Polissi, A. / Martorana, A. / Sperandeo, P. / Bolognesi, M. / Nardini, M.
CitationJournal: FEBS J. / Year: 2015
Title: Crystal Structure of Lpth, the Periplasmic Component of the Lipopolysaccharide Transport Machinery from Pseudomonas Aeruginosa.
Authors: Bollati, M. / Villa, R. / Gourlay, L.J. / Benedet, M. / Deho, G. / Polissi, A. / Barbiroli, A. / Martorana, A.M. / Sperandeo, P. / Bolognesi, M. / Marco, N.
History
DepositionJul 24, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 25, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 3, 2015Group: Database references
Revision 1.2Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PERIPLASMIC LIPOPOLYSACCHARIDE TRANSPORT PROTEIN LPTH


Theoretical massNumber of molelcules
Total (without water)19,1481
Polymers19,1481
Non-polymers00
Water57632
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)45.000, 45.000, 146.660
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein PERIPLASMIC LIPOPOLYSACCHARIDE TRANSPORT PROTEIN LPTH


Mass: 19147.742 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Strain: PAO1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): M15PREP4 / References: UniProt: Q9HVV7
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 32 / 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: 1.94 Å3/Da / Density % sol: 40.6 % / Description: NONE
Crystal growpH: 7.5
Details: 20% 1,4-BUTANEDIOL, 0.1 M HEPES (PH 7.5), 0.2 M NACL.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97241
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97241 Å / Relative weight: 1
ReflectionResolution: 2.75→45 Å / Num. obs: 4383 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 7.8 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 13.2
Reflection shellResolution: 2.75→2.9 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 4 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8.1_1168)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2R19
Resolution: 2.751→43.02 Å / SU ML: 0.33 / σ(F): 1.37 / Phase error: 27.07 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2959 344 4.6 %
Rwork0.2351 --
obs0.2377 4331 99.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.751→43.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1106 0 0 32 1138
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0051120
X-RAY DIFFRACTIONf_angle_d0.9111518
X-RAY DIFFRACTIONf_dihedral_angle_d18.339429
X-RAY DIFFRACTIONf_chiral_restr0.07177
X-RAY DIFFRACTIONf_plane_restr0.005201
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7507-3.46540.27881740.24663581X-RAY DIFFRACTION100
3.4654-43.02570.30611700.22913526X-RAY DIFFRACTION99

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