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- PDB-1z98: Crystal structure of the spinach aquaporin SoPIP2;1 in a closed c... -

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Basic information

Entry
Database: PDB / ID: 1z98
TitleCrystal structure of the spinach aquaporin SoPIP2;1 in a closed conformation
Componentsaquaporin
KeywordsTRANSPORT PROTEIN / MEMBRANE PROTEIN / INTEGRAL MEMBRANE PROTEIN / PIP / ALPHA-HELICAL / AQUAPORIN
Function / homology
Function and homology information


water channel activity / plasmodesma / vacuole / identical protein binding / plasma membrane
Similarity search - Function
Glycerol uptake facilitator protein / Glycerol uptake facilitator protein. / Aquaporin transporter / Major intrinsic protein, conserved site / MIP family signature. / Major intrinsic protein / Major intrinsic protein / Aquaporin-like / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesSpinacia oleracea (spinach)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsTornroth-Horsefield, S. / Hedfalk, K. / Johanson, U. / Karlsson, M. / Neutze, R. / Kjellbom, P.
CitationJournal: Nature / Year: 2006
Title: Structural mechanism of plant aquaporin gating
Authors: Tornroth-Horsefield, S. / Wang, Y. / Hedfalk, K. / Johanson, U. / Karlsson, M. / Tajkhorshid, E. / Neutze, R. / Kjellbom, P.
History
DepositionApr 1, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 20, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 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: aquaporin
M: aquaporin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,0844
Polymers59,8602
Non-polymers2252
Water3,603200
1
A: aquaporin
hetero molecules

A: aquaporin
hetero molecules

A: aquaporin
hetero molecules

A: aquaporin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,1698
Polymers119,7194
Non-polymers4504
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation3_655-y+1,x,z1
crystal symmetry operation4_565y,-x+1,z1
Buried area14680 Å2
ΔGint-190 kcal/mol
Surface area31280 Å2
MethodPISA, PQS
2
M: aquaporin
hetero molecules

M: aquaporin
hetero molecules

M: aquaporin
hetero molecules

M: aquaporin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,1698
Polymers119,7194
Non-polymers4504
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-x+1,-y+1,z1
crystal symmetry operation3_655-y+1,x,z1
crystal symmetry operation4_565y,-x+1,z1
Buried area14660 Å2
ΔGint-193 kcal/mol
Surface area31060 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)90.097, 90.097, 189.181
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number79
Cell settingtetragonal
Space group name H-MI4
Components on special symmetry positions
IDModelComponents
11A-1003-

HOH

21A-1087-

HOH

31M-2002-

HOH

41M-2088-

HOH

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Components

#1: Protein aquaporin


Mass: 29929.814 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Spinacia oleracea (spinach) / Production host: Pichia pastoris (fungus) / Strain (production host): X33 / References: UniProt: Q41372
#2: Chemical ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cd
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 200 / 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: 3.4 Å3/Da / Density % sol: 63.8 %

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.978 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 21, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 2.1→81.65 Å / Num. all: 53842 / Num. obs: 41491 / % possible obs: 99.74 % / Observed criterion σ(I): 1

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
REFMAC5.1.24refinement
CCP4(SCALA)data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→40 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.944 / SU B: 3.586 / SU ML: 0.096 / Cross valid method: THROUGHOUT / ESU R: 0.142 / ESU R Free: 0.138 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20847 2196 5 %RANDOM
Rwork0.18141 ---
obs0.1828 41486 99.74 %-
all-53842 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 30.236 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å20 Å20 Å2
2---0.04 Å20 Å2
3---0.08 Å2
Refinement stepCycle: LAST / Resolution: 2.1→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3756 0 2 200 3958
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0223862
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5441.9375266
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.7595500
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.05122130
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.19615556
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.0261514
X-RAY DIFFRACTIONr_chiral_restr0.1130.2608
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.022884
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2310.22025
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3150.22792
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1760.2201
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0020.21
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2720.2134
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.5230.218
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.317 169 -
Rwork0.236 3057 -
obs--100 %

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