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- PDB-1b27: STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE -

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Basic information

Entry
Database: PDB / ID: 1b27
TitleSTRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE
Components
  • PROTEIN (BARNASE)
  • PROTEIN (BARSTAR)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / RNASE-INHIBITOR COMPLEX / HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Function / homology
Function and homology information


Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region / cytoplasm
Similarity search - Function
Barstar-like / Barstar (barnase inhibitor) / Barstar (barnase inhibitor) / Barstar-like superfamily / Barnase; Chain D / Barnase / Guanine-specific ribonuclease N1/T1/U2 / ribonuclease / Microbial ribonucleases / Ribonuclease/ribotoxin ...Barstar-like / Barstar (barnase inhibitor) / Barstar (barnase inhibitor) / Barstar-like superfamily / Barnase; Chain D / Barnase / Guanine-specific ribonuclease N1/T1/U2 / ribonuclease / Microbial ribonucleases / Ribonuclease/ribotoxin / Nuclear Transport Factor 2; Chain: A, / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Ribonuclease / Barstar
Similarity search - Component
Biological speciesBacillus amyloliquefaciens (bacteria)
MethodX-RAY DIFFRACTION / OTHER / Resolution: 2.1 Å
AuthorsVaughan, C.K. / Buckle, A.M. / Fersht, A.R.
Citation
Journal: J.Mol.Biol. / Year: 1999
Title: Structural response to mutation at a protein-protein interface.
Authors: Vaughan, C.K. / Buckle, A.M. / Fersht, A.R.
#1: Journal: Biochemistry / Year: 1994
Title: Protein-Protein Recognition: Crystal Structural Analysis of a Barnase-Barstar Complex at 2.0-A Resolution
Authors: Buckle, A.M. / Schreiber, G. / Fersht, A.R.
#2: Journal: Structure / Year: 1994
Title: Stability and Function: Two Constraints in the Evolution of Barstar and Other Proteins
Authors: Schreiber, G. / Buckle, A.M. / Fersht, A.R.
#3: Journal: Structure / Year: 1993
Title: Recognition between a Bacterial Ribonuclease, Barnase, and its Natural Inhibitor, Barstar
Authors: Guillet, V. / Lapthorn, A. / Hartley, R.W. / Mauguen, Y.
#4: Journal: Biochemistry / Year: 1993
Title: Interaction of Barnase with its Polypeptide Inhibitor Barstar Studied by Protein Engineering
Authors: Schreiber, G. / Fersht, A.R.
#5: Journal: Nature / Year: 1982
Title: Molecular Structures of a New Family of Ribonucleases
Authors: Mauguen, Y. / Hartley, R.W. / Dodson, E.J. / Dodson, G.G. / Bricogne, G. / Chothia, C. / Jack, A.
History
DepositionDec 4, 1998Deposition site: PDBE / Processing site: RCSB
SupersessionDec 9, 1998ID: 1BV0
Revision 1.0Dec 9, 1998Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Aug 9, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (BARNASE)
B: PROTEIN (BARNASE)
C: PROTEIN (BARNASE)
D: PROTEIN (BARSTAR)
E: PROTEIN (BARSTAR)
F: PROTEIN (BARSTAR)


Theoretical massNumber of molelcules
Total (without water)68,0626
Polymers68,0626
Non-polymers00
Water9,224512
1
A: PROTEIN (BARNASE)
D: PROTEIN (BARSTAR)


Theoretical massNumber of molelcules
Total (without water)22,6872
Polymers22,6872
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: PROTEIN (BARNASE)
E: PROTEIN (BARSTAR)


Theoretical massNumber of molelcules
Total (without water)22,6872
Polymers22,6872
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: PROTEIN (BARNASE)
F: PROTEIN (BARSTAR)


Theoretical massNumber of molelcules
Total (without water)22,6872
Polymers22,6872
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)202.917, 43.319, 83.177
Angle α, β, γ (deg.)90.00, 110.50, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.246918, -0.89334, 0.375467), (-0.88996, 0.05575, -0.452618), (0.383409, -0.44591, -0.808802)36.581, 45.1, 35.884
2given(0.591389, -0.047755, 0.804971), (-0.085489, -0.996332, 0.003698), (0.801842, -0.071003, -0.593303)-16.968, 85.844, 23.516
3given(-0.229994, -0.873017, 0.430052), (-0.883858, 0.002435, -0.467749), (0.407305, -0.487684, -0.772183)35.9436, 47.004, 35.2867
4given(0.617301, -0.018178, 0.786517), (-0.029937, -0.999552, 0.000395), (0.786157, -0.02379, -0.617568)-19.268, 83.012, 25.203

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Components

#1: Protein PROTEIN (BARNASE)


Mass: 12398.721 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Cellular location: EXTRACELLULARGlossary of biology / Plasmid: PMT410 / Production host: Escherichia coli (E. coli) / Strain (production host): TG2 / References: UniProt: P00648, EC: 3.1.27.3
#2: Protein PROTEIN (BARSTAR)


Mass: 10288.608 Da / Num. of mol.: 3 / Mutation: C40A, C82A
Source method: isolated from a genetically manipulated source
Details: BARSTAR C(40,82)A IS REFERRED TO AS PSEUDO WILD-TYPE
Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Cellular location: CYTOSOL / Plasmid: PML2BS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)[PLYSE] / References: UniProt: P11540
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 512 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTER SER: THE ORIGINAL SEQUENCE OF BARSTAR OMITTED AN N-TERMINAL METHIONINE, WHICH WAS VISIBLE IN ...TER SER: THE ORIGINAL SEQUENCE OF BARSTAR OMITTED AN N-TERMINAL METHIONINE, WHICH WAS VISIBLE IN THE ELECTRON DENSITY. THE ORIGINAL SEQUENCE THEREFORE LISTS SER 89 AS THE C-TERMINUS. IN THIS STRUCTURE SER 90 IS THE C-TERMINAL RESIDUE

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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: 2.5 Å3/Da / Density % sol: 51 %
Description: THE STRUCTURE WAS SOLVED BY RIGID-BODY REFINEMENT OF PDB ENTRY 1BRS IN THE ASYMMETRIC UNIT
Crystal growpH: 8
Details: 18-24% PEG-8K 0.2 M AMMONIUM SULPHATE 0.1 M TRIS PH8.0
Crystal
*PLUS
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
118-24 %(w/v)PEG80001reservoir
20.2 Mammonium sulfate1reservoir
30.1 MTris1reservoir
420 mg/mlprotein1drop

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: ELLIOTT GX-13 / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1996 / Details: SUPER DOUBLE MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.08→24.11 Å / Num. obs: 32841 / % possible obs: 79.8 % / Redundancy: 2.4 % / Biso Wilson estimate: 26.38 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 10.4
Reflection shellResolution: 2.08→2.13 Å / Redundancy: 2 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 3.32 / % possible all: 65.4
Reflection shell
*PLUS
% possible obs: 65.4 % / Rmerge(I) obs: 0.357

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Processing

Software
NameVersionClassification
X-PLORmodel building
REFMACrefinement
MOSFLMdata reduction
CCP4(SCALA)data scaling
X-PLORphasing
RefinementMethod to determine structure: OTHER
Starting model: PDB ENTRY 1BRS

1brs


Resolution: 2.1→24 Å / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflection
Rfree0.259 -5 %
Rwork0.195 --
obs-30622 79.8 %
Displacement parametersBiso mean: 28.76 Å2
Refinement stepCycle: LAST / Resolution: 2.1→24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4598 0 0 512 5110
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0090.02
X-RAY DIFFRACTIONp_angle_d0.0270.04
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.0270.05
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it1.2092
X-RAY DIFFRACTIONp_mcangle_it1.8823
X-RAY DIFFRACTIONp_scbond_it1.3222
X-RAY DIFFRACTIONp_scangle_it1.9663
X-RAY DIFFRACTIONp_plane_restr
X-RAY DIFFRACTIONp_chiral_restr0.1030.15
X-RAY DIFFRACTIONp_singtor_nbd0.180.3
X-RAY DIFFRACTIONp_multtor_nbd0.2440.3
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd0.1330.3
X-RAY DIFFRACTIONp_planar_tor3.47
X-RAY DIFFRACTIONp_staggered_tor14.715
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor2720
X-RAY DIFFRACTIONp_special_tor15
Software
*PLUS
Name: REFMAC / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.1 Å / Lowest resolution: 24 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.195
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal target
X-RAY DIFFRACTIONp_bond_d0.02
X-RAY DIFFRACTIONp_angle_d0.04
X-RAY DIFFRACTIONp_mcbond_it2
X-RAY DIFFRACTIONp_scbond_it2
X-RAY DIFFRACTIONp_mcangle_it3
X-RAY DIFFRACTIONp_scangle_it3

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