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- PDB-1kxz: MT0146, the Precorrin-6y methyltransferase (CbiT) homolog from M.... -

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Basic information

Entry
Database: PDB / ID: 1kxz
TitleMT0146, the Precorrin-6y methyltransferase (CbiT) homolog from M. Thermoautotrophicum, P1 spacegroup
ComponentsPrecorrin-6y methyltransferase/putative decarboxylase
KeywordsTRANSFERASE / LYASE / structural genomics / beta barrel / rossmann fold / tetramer / methyltransferase / decarboxylase
Function / homology
Function and homology information


cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating] / cobalt-precorrin-6B C5-methyltransferase activity / anaerobic cobalamin biosynthetic process / protein methyltransferase activity / methylation
Similarity search - Function
Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) CbiT / Cobalamin biosynthesis, precorrin-6Y methyltransferase, CbiT subunit / : / Methyltransferase domain / Methyltransferase domain / Vaccinia Virus protein VP39 / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)
Similarity search - Component
Biological speciesMethanothermobacter thermautotrophicus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsKeller, J.P. / Smith, P.M. / Benach, J. / Christendat, D. / DeTitta, G. / Hunt, J.F.
CitationJournal: Structure / Year: 2002
Title: The Crystal Structure of MT0146/CbiT Suggests that the Putative Precorrin-8W Decarboxylase is a Methyltransferase
Authors: Keller, J.P. / Smith, P.M. / Benach, J. / Christendat, D. / DeTitta, G. / Hunt, J.F.
History
DepositionFeb 1, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 27, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 16, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.4Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.5Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Precorrin-6y methyltransferase/putative decarboxylase
B: Precorrin-6y methyltransferase/putative decarboxylase
C: Precorrin-6y methyltransferase/putative decarboxylase
D: Precorrin-6y methyltransferase/putative decarboxylase
E: Precorrin-6y methyltransferase/putative decarboxylase
F: Precorrin-6y methyltransferase/putative decarboxylase
G: Precorrin-6y methyltransferase/putative decarboxylase
H: Precorrin-6y methyltransferase/putative decarboxylase


Theoretical massNumber of molelcules
Total (without water)168,8978
Polymers168,8978
Non-polymers00
Water2,000111
1
A: Precorrin-6y methyltransferase/putative decarboxylase
B: Precorrin-6y methyltransferase/putative decarboxylase
C: Precorrin-6y methyltransferase/putative decarboxylase
D: Precorrin-6y methyltransferase/putative decarboxylase


Theoretical massNumber of molelcules
Total (without water)84,4494
Polymers84,4494
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7450 Å2
ΔGint-68 kcal/mol
Surface area27870 Å2
MethodPISA
2
E: Precorrin-6y methyltransferase/putative decarboxylase
F: Precorrin-6y methyltransferase/putative decarboxylase
G: Precorrin-6y methyltransferase/putative decarboxylase
H: Precorrin-6y methyltransferase/putative decarboxylase


Theoretical massNumber of molelcules
Total (without water)84,4494
Polymers84,4494
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7420 Å2
ΔGint-69 kcal/mol
Surface area27870 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.100, 76.000, 97.200
Angle α, β, γ (deg.)70.90, 78.80, 66.70
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Precorrin-6y methyltransferase/putative decarboxylase / MT0146 / cbiT / MTH146


Mass: 21112.131 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea)
Gene: MTH146 / Plasmid: B834 Codon+ / Production host: Escherichia coli (E. coli) / References: UniProt: O26249
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 111 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.24 Å3/Da / Density % sol: 44.99 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PEG8000, magnesium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystal grow
*PLUS
Temperature: 25 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
15-10 mg/mlprotein1drop
210 %(w/v)PEG80001drop
3100 mM1dropMgCl2
45 mMTris-Cl1droppH7.5
516-22 %PEG80001reservoir
6200 mM1reservoirMgCl2
710 mMTris-Cl1reservoirpH7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97956
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 15, 2000
RadiationMonochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97956 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 39161 / % possible obs: 98.8 % / Observed criterion σ(F): -2 / Observed criterion σ(I): -2 / Redundancy: 1.91 %
Reflection shellResolution: 2.7→2.77 Å / % possible all: 97.6
Reflection
*PLUS
Highest resolution: 2.64 Å / Lowest resolution: 40 Å / Rmerge(I) obs: 0.15
Reflection shell
*PLUS
% possible obs: 97.3 % / Mean I/σ(I) obs: 1.7

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLOR3.851refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1f38

1f38


Resolution: 2.7→36.65 Å / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.257 1672 random
Rwork0.212 --
obs-33438 -
Refinement stepCycle: LAST / Resolution: 2.7→36.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11136 0 0 111 11247
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_angle_deg1.77
X-RAY DIFFRACTIONx_bond_d0.015
Refinement
*PLUS
Highest resolution: 2.64 Å / Lowest resolution: 40 Å / Rfactor Rfree: 0.2572 / Rfactor Rwork: 0.212
Solvent computation
*PLUS
Displacement parameters
*PLUS

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