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- PDB-8eov: Precisely patterned nanofibers made from extendable protein multi... -

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Basic information

Entry
Database: PDB / ID: 8eov
TitlePrecisely patterned nanofibers made from extendable protein multiplexes
ComponentsC2HR1_4r
KeywordsDE NOVO PROTEIN / de novo design / nanofibers
Function / homologyPHOSPHATE ION
Function and homology information
Biological speciessynthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.59 Å
AuthorsBera, A.K. / Bethel, N.P.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nat Chem / Year: 2023
Title: Precisely patterned nanofibres made from extendable protein multiplexes.
Authors: Neville P Bethel / Andrew J Borst / Fabio Parmeggiani / Matthew J Bick / T J Brunette / Hannah Nguyen / Alex Kang / Asim K Bera / Lauren Carter / Marcos C Miranda / Ryan D Kibler / Mila Lamb ...Authors: Neville P Bethel / Andrew J Borst / Fabio Parmeggiani / Matthew J Bick / T J Brunette / Hannah Nguyen / Alex Kang / Asim K Bera / Lauren Carter / Marcos C Miranda / Ryan D Kibler / Mila Lamb / Xinting Li / Banumathi Sankaran / David Baker /
Abstract: Molecular systems with coincident cyclic and superhelical symmetry axes have considerable advantages for materials design as they can be readily lengthened or shortened by changing the length of the ...Molecular systems with coincident cyclic and superhelical symmetry axes have considerable advantages for materials design as they can be readily lengthened or shortened by changing the length of the constituent monomers. Among proteins, alpha-helical coiled coils have such symmetric, extendable architectures, but are limited by the relatively fixed geometry and flexibility of the helical protomers. Here we describe a systematic approach to generating modular and rigid repeat protein oligomers with coincident C to C and superhelical symmetry axes that can be readily extended by repeat propagation. From these building blocks, we demonstrate that a wide range of unbounded fibres can be systematically designed by introducing hydrophilic surface patches that force staggering of the monomers; the geometry of such fibres can be precisely tuned by varying the number of repeat units in the monomer and the placement of the hydrophilic patches.
History
DepositionOct 4, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 16, 2023Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Dec 20, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: C2HR1_4r
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,0906
Polymers17,6151
Non-polymers4755
Water75742
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)49.140, 49.140, 111.211
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Space group name HallP322"
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
#4: x-y,-y,-z+1/3
#5: -x,-x+y,-z+2/3
#6: y,x,-z

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Components

#1: Protein C2HR1_4r


Mass: 17614.869 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#2: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: PO4 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 42 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.2 Å3/Da / Density % sol: 44.1 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M MES pH 6.0, 3.2 M Ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 0.97 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 15, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 1.59→42.56 Å / Num. obs: 21628 / % possible obs: 99.76 % / Redundancy: 2 % / Biso Wilson estimate: 31.39 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.0134 / Net I/σ(I): 23.39
Reflection shellResolution: 1.59→1.64 Å / Redundancy: 2 % / Rmerge(I) obs: 1.038 / Mean I/σ(I) obs: 0.68 / Num. unique obs: 2120 / CC1/2: 0.389 / % possible all: 99.67

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Processing

Software
NameVersionClassification
PHENIX1.19.1_4122refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Designed model

Resolution: 1.59→42.56 Å / SU ML: 0.2523 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 32.1333
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2246 1995 9.24 %
Rwork0.2029 19597 -
obs0.205 21592 99.76 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 46.11 Å2
Refinement stepCycle: LAST / Resolution: 1.59→42.56 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1181 0 25 42 1248
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061215
X-RAY DIFFRACTIONf_angle_d0.62311643
X-RAY DIFFRACTIONf_chiral_restr0.0426202
X-RAY DIFFRACTIONf_plane_restr0.0053205
X-RAY DIFFRACTIONf_dihedral_angle_d14.7157499
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.59-1.630.37951420.39561374X-RAY DIFFRACTION99.74
1.63-1.670.37821400.3731354X-RAY DIFFRACTION99.73
1.67-1.720.36851400.3551371X-RAY DIFFRACTION99.87
1.72-1.780.38981380.33371384X-RAY DIFFRACTION99.8
1.78-1.840.31961410.27711378X-RAY DIFFRACTION99.8
1.84-1.920.33041400.27281372X-RAY DIFFRACTION99.6
1.92-20.26941430.25371380X-RAY DIFFRACTION99.48
2-2.110.28371450.21341389X-RAY DIFFRACTION99.93
2.11-2.240.23721400.20371408X-RAY DIFFRACTION99.74
2.24-2.410.2631400.18411381X-RAY DIFFRACTION100
2.41-2.660.21441390.20081417X-RAY DIFFRACTION100
2.66-3.040.20911450.2011438X-RAY DIFFRACTION100
3.04-3.830.19331440.18821435X-RAY DIFFRACTION100
3.83-42.560.19461580.17641516X-RAY DIFFRACTION99.17
Refinement TLS params.Method: refined / Origin x: -28.8783876116 Å / Origin y: 18.4154849582 Å / Origin z: 6.7860626823 Å
111213212223313233
T0.244433284698 Å20.103948061568 Å20.00595379043352 Å2-0.323107463628 Å20.028008986958 Å2--0.178442999275 Å2
L4.0507328736 °21.31014830241 °20.0128679209968 °2-1.96915468883 °20.0201641292095 °2--2.91660558081 °2
S0.027246468221 Å °-0.00877196830951 Å °-0.257927469537 Å °0.00568241206105 Å °-0.104520675468 Å °-0.171393963484 Å °0.257326793289 Å °0.373988627353 Å °0.0880152084221 Å °
Refinement TLS groupSelection details: all

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