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- PDB-5a9x: Structure of GDP bound BipA -

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Basic information

Entry
Database: PDB / ID: 5a9x
TitleStructure of GDP bound BipA
ComponentsGTP-BINDING PROTEING protein
KeywordsRIBOSOMAL PROTEIN / BIPA / RIBOSOME / TRANSLATIONAL GTPASE FACTORS
Function / homology
Function and homology information


guanosine tetraphosphate binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / ribosome binding / ribosome biogenesis / tRNA binding / rRNA binding / ribonucleoprotein complex / GTPase activity / GTP binding / cytosol / cytoplasm
Similarity search - Function
: / : / : / : / TypA/BipA C-terminal domain / GTP-binding protein TypA / BipA, domain V / GTP-binding protein TypA/BipA, C-terminal / Elongation factor EFG, domain V-like / Elongation factor G C-terminus ...: / : / : / : / TypA/BipA C-terminal domain / GTP-binding protein TypA / BipA, domain V / GTP-binding protein TypA/BipA, C-terminal / Elongation factor EFG, domain V-like / Elongation factor G C-terminus / EF-G domain III/V-like / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Large ribosomal subunit assembly factor BipA / Large ribosomal subunit assembly factor BipA
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 3.8 Å
AuthorsKumar, V. / Chen, Y. / Ero, R. / Li, Z. / Gao, Y.-G.
CitationJournal: Proc Natl Acad Sci U S A / Year: 2015
Title: Structure of BipA in GTP form bound to the ratcheted ribosome.
Authors: Veerendra Kumar / Yun Chen / Rya Ero / Tofayel Ahmed / Jackie Tan / Zhe Li / Andrew See Weng Wong / Shashi Bhushan / Yong-Gui Gao /
Abstract: BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly ...BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation.
History
DepositionJul 23, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 26, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 2, 2015Group: Database references
Revision 1.2Sep 16, 2015Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GTP-BINDING PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8832
Polymers67,4391
Non-polymers4431
Water181
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)241.946, 241.946, 241.946
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number214
Space group name H-MI4132

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Components

#1: Protein GTP-BINDING PROTEIN / G protein / BIPA


Mass: 67439.312 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: TRANSLATIONAL GTPASE / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA T1R / References: UniProt: B7MHF0, UniProt: P0DTT0*PLUS
#2: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1 / 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: 2.14 Å3/Da / Density % sol: 42.5 % / Description: NONE
Crystal growDetails: 20% (W/V) PEG3350, 0.2 M SODIUM FLUORIDE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 8, 2015
RadiationMonochromator: LN2 COOLED FIXED-EXIT SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.8→47.45 Å / Num. obs: 10596 / % possible obs: 99.6 % / Observed criterion σ(I): 1 / Redundancy: 17.8 % / Rmerge(I) obs: 0.17 / Net I/σ(I): 14.96

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Processing

Software
NameVersionClassification
REFMAC5.8.0107refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: OTHER
Starting model: NONE

Resolution: 3.8→47.45 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.919 / SU B: 89.909 / SU ML: 1.033 / Cross valid method: THROUGHOUT / ESU R Free: 0.783 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.31268 1176 10 %RANDOM
Rwork0.24779 ---
obs0.25426 10584 96.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 240.067 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 3.8→47.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4138 0 28 1 4167
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0194224
X-RAY DIFFRACTIONr_bond_other_d0.0020.024055
X-RAY DIFFRACTIONr_angle_refined_deg1.5211.9715745
X-RAY DIFFRACTIONr_angle_other_deg1.06639291
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.585550
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.61125.027187
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.57715672
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.5411527
X-RAY DIFFRACTIONr_chiral_restr0.0820.2681
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0214867
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02904
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it12.88423.8772218
X-RAY DIFFRACTIONr_mcbond_other12.88423.8762217
X-RAY DIFFRACTIONr_mcangle_it21.15135.7842762
X-RAY DIFFRACTIONr_mcangle_other21.14735.7852763
X-RAY DIFFRACTIONr_scbond_it10.56124.5182002
X-RAY DIFFRACTIONr_scbond_other10.55624.5151994
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other18.31236.5282970
X-RAY DIFFRACTIONr_long_range_B_refined28.5734616
X-RAY DIFFRACTIONr_long_range_B_other28.5784614
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3.801→3.899 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.703 60 -
Rwork0.695 539 -
obs--67.91 %

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