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- PDB-7sea: Crystal structure of human Fibrillarin in complex with compound 2... -

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Basic information

Entry
Database: PDB / ID: 7sea
TitleCrystal structure of human Fibrillarin in complex with compound 2 from cocktail soak
ComponentsrRNA 2'-O-methyltransferase fibrillarin
KeywordsTRANSFERASE / Methyltransferase / S-adenosyl methionine
Function / homology
Function and homology information


U6 snRNA 2'-O-ribose methyltransferase activity / snoRNA localization / granular component / histone H2AQ104 methyltransferase activity / box C/D sno(s)RNA 3'-end processing / rRNA methyltransferase activity / box C/D methylation guide snoRNP complex / rRNA methylation / rRNA modification in the nucleus and cytosol / TFIID-class transcription factor complex binding ...U6 snRNA 2'-O-ribose methyltransferase activity / snoRNA localization / granular component / histone H2AQ104 methyltransferase activity / box C/D sno(s)RNA 3'-end processing / rRNA methyltransferase activity / box C/D methylation guide snoRNP complex / rRNA methylation / rRNA modification in the nucleus and cytosol / TFIID-class transcription factor complex binding / Major pathway of rRNA processing in the nucleolus and cytosol / Cajal body / Transferases; Transferring one-carbon groups; Methyltransferases / small-subunit processome / fibrillar center / rRNA processing / osteoblast differentiation / ATPase binding / ribosomal small subunit biogenesis / nucleolus / RNA binding / extracellular exosome / nucleoplasm / nucleus / membrane
Similarity search - Function
rRNA 2'-O-methyltransferase fibrillarin-like / Fibrillarin, conserved site / Fibrillarin / Fibrillarin signature. / Fibrillarin / Vaccinia Virus protein VP39 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold ...rRNA 2'-O-methyltransferase fibrillarin-like / Fibrillarin, conserved site / Fibrillarin / Fibrillarin signature. / Fibrillarin / Vaccinia Virus protein VP39 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
6-(trifluoromethyl)pyrimidin-4-amine / FORMIC ACID / rRNA 2'-O-methyltransferase fibrillarin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.91 Å
AuthorsShi, Y. / El-Deeb, I.M. / Masic, V. / Hartley-Tassell, L. / Maggioni, A. / von Itzstein, M. / Ve, T.
Funding support Australia, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia) Australia
Australian Research Council (ARC) Australia
CitationJournal: Pharmaceuticals / Year: 2021
Title: Discovery of Cofactor Competitive Inhibitors against the Human Methyltransferase Fibrillarin.
Authors: Shi, Y. / El-Deeb, I.M. / Masic, V. / Hartley-Tassell, L. / Maggioni, A. / Itzstein, M.V. / Ve, T.
History
DepositionSep 30, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 9, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 18, 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

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Assembly

Deposited unit
A: rRNA 2'-O-methyltransferase fibrillarin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,1538
Polymers26,6821
Non-polymers4717
Water1,69394
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)69.131, 138.651, 66.426
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Space group name HallC2c2
Symmetry operation#1: x,y,z
#2: x,-y,-z
#3: -x,y,-z+1/2
#4: -x,-y,z+1/2
#5: x+1/2,y+1/2,z
#6: x+1/2,-y+1/2,-z
#7: -x+1/2,y+1/2,-z+1/2
#8: -x+1/2,-y+1/2,z+1/2

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Components

#1: Protein rRNA 2'-O-methyltransferase fibrillarin / 34 kDa nucleolar scleroderma antigen / Histone-glutamine methyltransferase / U6 snRNA 2'-O- ...34 kDa nucleolar scleroderma antigen / Histone-glutamine methyltransferase / U6 snRNA 2'-O-methyltransferase fibrillarin


Mass: 26681.590 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FBL, FIB1, FLRN / Production host: Escherichia coli (E. coli)
References: UniProt: P22087, Transferases; Transferring one-carbon groups; Methyltransferases
#2: Chemical
ChemComp-FMT / FORMIC ACID


Mass: 46.025 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: CH2O2
#3: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#4: Chemical ChemComp-8XF / 6-(trifluoromethyl)pyrimidin-4-amine


Mass: 163.101 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H4F3N3 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 94 / 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: 2.98 Å3/Da / Density % sol: 58.76 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 2.75-3.3 M Sodium Formate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 7, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.91→47.96 Å / Num. obs: 25161 / % possible obs: 99.8 % / Redundancy: 7.3 % / Biso Wilson estimate: 27.34 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.059 / Rpim(I) all: 0.023 / Rrim(I) all: 0.063 / Net I/σ(I): 17.4
Reflection shellResolution: 1.91→1.95 Å / Rmerge(I) obs: 0.833 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 1639 / CC1/2: 0.865 / Rpim(I) all: 0.334 / Rrim(I) all: 0.899

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Processing

Software
NameVersionClassification
PHENIX1.19.1_4122refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2IPX

2ipx


Resolution: 1.91→45.27 Å / SU ML: 0.2289 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.9043
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2289 2000 7.96 %
Rwork0.1957 23138 -
obs0.1984 25138 99.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 33.75 Å2
Refinement stepCycle: LAST / Resolution: 1.91→45.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1777 0 30 94 1901
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01111838
X-RAY DIFFRACTIONf_angle_d1.07562484
X-RAY DIFFRACTIONf_chiral_restr0.0691280
X-RAY DIFFRACTIONf_plane_restr0.0093329
X-RAY DIFFRACTIONf_dihedral_angle_d13.531680
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.91-1.960.34521390.28011618X-RAY DIFFRACTION97.5
1.96-2.010.26611400.23841599X-RAY DIFFRACTION99.94
2.01-2.070.2831400.22451638X-RAY DIFFRACTION100
2.07-2.140.26271430.21881644X-RAY DIFFRACTION100
2.14-2.210.27051400.2161628X-RAY DIFFRACTION100
2.21-2.30.27161420.2071631X-RAY DIFFRACTION99.61
2.3-2.410.24631420.20231644X-RAY DIFFRACTION100
2.41-2.530.25931420.20991645X-RAY DIFFRACTION100
2.53-2.690.20851430.20941648X-RAY DIFFRACTION99.94
2.69-2.90.23211440.20731671X-RAY DIFFRACTION99.94
2.9-3.190.26521430.21151657X-RAY DIFFRACTION100
3.19-3.650.22881440.18691663X-RAY DIFFRACTION99.89
3.65-4.60.16051450.1571684X-RAY DIFFRACTION100
4.6-45.270.2191530.18331768X-RAY DIFFRACTION99.64

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