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- PDB-2d62: Crystal structure of multiple sugar binding transport ATP-binding... -

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Basic information

Entry
Database: PDB / ID: 2d62
TitleCrystal structure of multiple sugar binding transport ATP-binding protein
Componentsmultiple sugar-binding transport ATP-binding protein
KeywordsSUGAR BINDING PROTEIN / ATP-binding / Structural geomics / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


ATP hydrolysis activity / ATP binding / membrane
Similarity search - Function
Transport-associated OB, type 1 / TOBE domain / MalK, OB fold domain / MalK OB fold domain / Molybdate/tungstate binding, C-terminal / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Nucleic acid-binding proteins / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter ...Transport-associated OB, type 1 / TOBE domain / MalK, OB fold domain / MalK OB fold domain / Molybdate/tungstate binding, C-terminal / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Nucleic acid-binding proteins / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PYROPHOSPHATE 2- / 375aa long hypothetical multiple sugar-binding transport ATP-binding protein
Similarity search - Component
Biological speciesPyrococcus horikoshii (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.1 Å
AuthorsLokanath, N.K. / Mizohata, E. / Yamaguchi-Sihta, E. / Chen, L. / Liu, Z.J. / Wang, B.C. / Kunishima, N. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be Published
Title: Crystal structure of multiple sugar binding transport ATP-binding protein
Authors: Lokanath, N.K. / Mizohata, E. / Yamaguchi-Sihta, E. / Chen, L. / Liu, Z.J. / Wang, B.C. / Kunishima, N.
History
DepositionNov 8, 2005Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 8, 2006Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: 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: multiple sugar-binding transport ATP-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,0769
Polymers43,2281
Non-polymers8488
Water6,071337
1
A: multiple sugar-binding transport ATP-binding protein
hetero molecules

A: multiple sugar-binding transport ATP-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,15218
Polymers86,4562
Non-polymers1,69716
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation12_565x,x-y+1,-z+1/61
Unit cell
Length a, b, c (Å)119.304, 119.304, 180.503
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11A-1414-

HOH

DetailsBiologically this protein is dimer.

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Components

#1: Protein multiple sugar-binding transport ATP-binding protein


Mass: 43227.816 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 CodonPlus(DE3)-RIL / References: UniProt: O57933
#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-POP / PYROPHOSPHATE 2- / Pyrophosphate


Mass: 175.959 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: H2O7P2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 337 / 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: 4.29 Å3/Da / Density % sol: 71.31 %
Crystal growTemperature: 295 K / Method: microbatch / pH: 4.5
Details: Sodium Citrate, Ammonium sulfate, Lithium sulfate, pH 4.5, MICROBATCH, temperature 295.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.97243 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 23, 2005
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97243 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. all: 44743 / Num. obs: 44713 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 16.6 % / Biso Wilson estimate: 19 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 10.5
Reflection shellResolution: 2.1→2.18 Å / % possible all: 98.6

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Processing

Software
NameVersionClassification
CNS1.1refinement
HKL-2000data reduction
SCALEPACKdata scaling
SOLVEphasing
RefinementMethod to determine structure: SAD / Resolution: 2.1→44.84 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2866843.6 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.214 2247 5 %RANDOM
Rwork0.198 ---
obs0.198 44710 99.6 %-
all-44743 --
Solvent computationSolvent model: FLAT MODEL / Bsol: 53.8011 Å2 / ksol: 0.378422 e/Å3
Displacement parametersBiso mean: 34.6 Å2
Baniso -1Baniso -2Baniso -3
1-0.31 Å20.57 Å20 Å2
2--0.31 Å20 Å2
3----0.63 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.25 Å0.22 Å
Luzzati d res low-5 Å
Luzzati sigma a0.21 Å0.18 Å
Refinement stepCycle: LAST / Resolution: 2.1→44.84 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2988 0 44 337 3369
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.005
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_dihedral_angle_d23.7
X-RAY DIFFRACTIONc_improper_angle_d0.73
X-RAY DIFFRACTIONc_mcbond_it1.391.5
X-RAY DIFFRACTIONc_mcangle_it2.22
X-RAY DIFFRACTIONc_scbond_it2.582
X-RAY DIFFRACTIONc_scangle_it3.712.5
LS refinement shellResolution: 2.1→2.23 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.247 365 5.1 %
Rwork0.228 6808 -
obs--97.9 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1protein_rep.paramprotein.top
X-RAY DIFFRACTION2water_rep.paramwater.top
X-RAY DIFFRACTION3ion.paramion.top
X-RAY DIFFRACTION4pop.parampop.top

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