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- PDB-1q7q: Cobalamin-dependent methionine synthase (1-566) from T. maritima ... -

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Basic information

Entry
Database: PDB / ID: 1q7q
TitleCobalamin-dependent methionine synthase (1-566) from T. maritima (Oxidized, Orthorhombic)
Components5-methyltetrahydrofolate S-homocysteine methyltransferase
KeywordsTRANSFERASE / homocysteine / methionine / folate / cobalamin / vitamin b12
Function / homology
Function and homology information


methionine synthase / methionine synthase activity / homocysteine metabolic process / methionine biosynthetic process / cobalamin binding / tetrahydrofolate metabolic process / methylation / metal ion binding / cytosol
Similarity search - Function
5-methyltetrahydrofolate-homocysteine S-methyltransferase, bacterial / Homocysteine-binding-like domain / B12-binding N-terminal domain profile. / B12 binding domain / Homocysteine-binding domain / Homocysteine-binding domain superfamily / Homocysteine S-methyltransferase / Homocysteine-binding domain profile. / : / Cobalamin (vitamin B12)-binding module, cap domain ...5-methyltetrahydrofolate-homocysteine S-methyltransferase, bacterial / Homocysteine-binding-like domain / B12-binding N-terminal domain profile. / B12 binding domain / Homocysteine-binding domain / Homocysteine-binding domain superfamily / Homocysteine S-methyltransferase / Homocysteine-binding domain profile. / : / Cobalamin (vitamin B12)-binding module, cap domain / B12 binding domain / Methionine synthase domain / B12 binding domain / Cobalamin-binding domain superfamily / B12-binding domain profile. / Cobalamin (vitamin B12)-binding domain / Dihydropteroate synthase-like / Pterin-binding domain / Pterin binding enzyme / Pterin-binding domain profile. / Dihydropteroate synthase-like / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Biological speciesThermotoga maritima (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsEvans, J.C. / Huddler, D.P. / Hilgers, M.T. / Romanchuk, G. / Matthews, R.G. / Ludwig, M.L.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2004
Title: Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
Authors: Evans, J.C. / Huddler, D.P. / Hilgers, M.T. / Romanchuk, G. / Matthews, R.G. / Ludwig, M.L.
History
DepositionAug 19, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 23, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software
Revision 1.4Oct 9, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 5-methyltetrahydrofolate S-homocysteine methyltransferase
B: 5-methyltetrahydrofolate S-homocysteine methyltransferase


Theoretical massNumber of molelcules
Total (without water)127,2662
Polymers127,2662
Non-polymers00
Water3,495194
1
A: 5-methyltetrahydrofolate S-homocysteine methyltransferase


Theoretical massNumber of molelcules
Total (without water)63,6331
Polymers63,6331
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: 5-methyltetrahydrofolate S-homocysteine methyltransferase


Theoretical massNumber of molelcules
Total (without water)63,6331
Polymers63,6331
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)92.583, 169.022, 174.276
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein 5-methyltetrahydrofolate S-homocysteine methyltransferase


Mass: 63633.148 Da / Num. of mol.: 2 / Fragment: MetH_Tm (residues 1-566)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (bacteria) / Plasmid: pET29a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21-DE3 / References: UniProt: Q9WYA5, methionine synthase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 194 / 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: 5.36 Å3/Da / Density % sol: 77.04 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.7
Details: propylene glycol, glycerol, PEG 8000, citrate, 1,2,3-heptanetriol, cadmium, pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Crystal grow
*PLUS
Temperature: 4 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
110 mM1dropCdCl2
21.25 %(w/v)1,2,3-heptanetriol1drop
325 %1,2-propanediol1reservoir
410 %glycerol1reservoir
55 %PEG30001reservoir
6100 mMsodium citrate1reservoirpH5.30

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 5ID-B / Wavelength: 1 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 12, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.1→50 Å / Num. all: 50378 / Num. obs: 45652 / % possible obs: 90.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shellResolution: 3.1→3.24 Å / % possible all: 71.8
Reflection
*PLUS
Highest resolution: 3.1 Å / % possible obs: 89.4 % / Redundancy: 2.6 % / Rmerge(I) obs: 0.074
Reflection shell
*PLUS
% possible obs: 63.6 % / Rmerge(I) obs: 0.263 / Mean I/σ(I) obs: 2.54

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Processing

Software
NameClassification
MAR345data collection
XDSdata reduction
CNSrefinement
XDSdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.1→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.265 4608 RANDOM THROUGHOUT
Rwork0.221 --
all0.253 50378 -
obs0.253 45652 -
Refinement stepCycle: LAST / Resolution: 3.1→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8837 0 0 194 9031
Refinement
*PLUS
% reflection Rfree: 10 % / Rfactor Rfree: 0.248 / Rfactor Rwork: 0.205
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONbond_d0.0077
X-RAY DIFFRACTIONangle_d
X-RAY DIFFRACTIONangle_deg1.36

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