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- PDB-1rg9: S-Adenosylmethionine synthetase complexed with SAM and PPNP -

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Basic information

Entry
Database: PDB / ID: 1rg9
TitleS-Adenosylmethionine synthetase complexed with SAM and PPNP
ComponentsS-adenosylmethionine synthetase
KeywordsTRANSFERASE / S-adenosylmethionine synthetase / methionine adenosyltransferase
Function / homology
Function and homology information


methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine cycle / S-adenosylmethionine biosynthetic process / potassium ion binding / one-carbon metabolic process / magnesium ion binding / ATP binding / identical protein binding / cytosol
Similarity search - Function
GMP Synthetase; Chain A, domain 3 - #10 / S-adenosylmethionine synthetase / S-adenosylmethionine synthetase, N-terminal / S-adenosylmethionine synthetase, central domain / S-adenosylmethionine synthetase, C-terminal / S-adenosylmethionine synthetase, conserved site / S-adenosylmethionine synthetase superfamily / S-adenosylmethionine synthetase, N-terminal domain / S-adenosylmethionine synthetase, central domain / S-adenosylmethionine synthetase, C-terminal domain ...GMP Synthetase; Chain A, domain 3 - #10 / S-adenosylmethionine synthetase / S-adenosylmethionine synthetase, N-terminal / S-adenosylmethionine synthetase, central domain / S-adenosylmethionine synthetase, C-terminal / S-adenosylmethionine synthetase, conserved site / S-adenosylmethionine synthetase superfamily / S-adenosylmethionine synthetase, N-terminal domain / S-adenosylmethionine synthetase, central domain / S-adenosylmethionine synthetase, C-terminal domain / S-adenosylmethionine synthase signature 1. / S-adenosylmethionine synthase signature 2. / GMP Synthetase; Chain A, domain 3 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
: / (DIPHOSPHONO)AMINOPHOSPHONIC ACID / S-ADENOSYLMETHIONINE / S-adenosylmethionine synthase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsKomoto, J. / Yamada, T. / Takata, Y. / Markham, G.D. / Takusagawa, F.
CitationJournal: Biochemistry / Year: 2004
Title: Crystal structure of the S-adenosylmethionine synthetase ternary complex: a novel catalytic mechanism of s-adenosylmethionine synthesis from ATP and MET.
Authors: Komoto, J. / Yamada, T. / Takata, Y. / Markham, G.D. / Takusagawa, F.
History
DepositionNov 11, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 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 1.4Apr 4, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type
Revision 1.5Feb 14, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 600HETEROGEN THE AUTHORS REFINED THE TWO COMPLEX STRUCTURES WITH ONE HKLFO DATA SET SINCE THE AUTHORS ...HETEROGEN THE AUTHORS REFINED THE TWO COMPLEX STRUCTURES WITH ONE HKLFO DATA SET SINCE THE AUTHORS COULD NOT DETERMINE THE CONTENTS IN THE ACTIVE SITE. THIS IS DESCRIBED IN THE PAPER. ONE MODEL (1P7L) CONTAINS AMPPNP AND MET IN DIMER AB AND SAM AND PPNP IN DIMER CD, AND THE OTHER MODEL (1RG9) CONTAINS SAM AND PPNP IN BOTH DIMERS. TWO MODELS WERE REFINED WITH THE HKLFO DATA DEPOSITED WITH 1RG9.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: S-adenosylmethionine synthetase
B: S-adenosylmethionine synthetase
C: S-adenosylmethionine synthetase
D: S-adenosylmethionine synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,44224
Polymers167,4694
Non-polymers2,97220
Water36020
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22520 Å2
ΔGint-143 kcal/mol
Surface area46220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)225.82, 69.13, 118.23
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121
DetailsThis enzyme is a homo-tetramer. The crystallographic asymmetric unit contains one tetramer.

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
S-adenosylmethionine synthetase / Methionine adenosyltransferase / AdoMet synthetase / MAT


Mass: 41867.309 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: METK, METX, B2942, C3528, Z4287, ECS3818, SF2933, S3137
Production host: Escherichia coli (E. coli) / References: UniProt: P0A817, methionine adenosyltransferase

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Non-polymers , 5 types, 40 molecules

#2: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: K
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-SAM / S-ADENOSYLMETHIONINE


Mass: 398.437 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H22N6O5S
#5: Chemical
ChemComp-PPK / (DIPHOSPHONO)AMINOPHOSPHONIC ACID


Mass: 256.970 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: H6NO9P3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O

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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: 2.75 Å3/Da / Density % sol: 55.34 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 8
Details: PEG-8000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 296K
Crystal grow
*PLUS
Temperature: 23 ℃ / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
18 %(v/w)PEG80001reservoir
250 mMTris-HCl1reservoirpH8.0
3200 mM1reservoirKCl
41 mMdithiothreitol1reservoir
520 %ethylene glycol1reservoir
650 mMHEPES-K+1drop
720 mg/mlprotein1drop

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 1, 2003 / Details: confocal optics
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. all: 46081 / Num. obs: 46081 / % possible obs: 95 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shellResolution: 2.5→2.6 Å / % possible all: 78
Reflection
*PLUS
% possible obs: 95 % / Num. measured all: 165302 / Rmerge(I) obs: 0.093
Reflection shell
*PLUS
Lowest resolution: 2.61 Å / Rmerge(I) obs: 0.187

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
X-PLORmodel building
X-PLOR3.851refinement
X-PLORphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→10 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
Details: The authors refined the two complex structures with one hklfo data set since the authors could not determine the contents in the active site. This is described in the paper. One model (1P7L) ...Details: The authors refined the two complex structures with one hklfo data set since the authors could not determine the contents in the active site. This is described in the paper. One model (1P7L) contains AMPPNP and Met in dimer AB and SAM and PPNP in dimer CD, and the other model (1RG9) contains SAM and PPNP in both dimers. Two models were refined with the hklfo data deposited with 1RG9.
RfactorNum. reflectionSelection details
Rfree0.241 4506 RANDOM
Rwork0.211 --
all0.212 40557 -
obs0.212 40557 -
Refinement stepCycle: LAST / Resolution: 2.5→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11768 0 172 20 11960
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_angle_deg1.36
X-RAY DIFFRACTIONx_dihedral_angle_d27.5
Refinement
*PLUS
Lowest resolution: 10 Å / Num. reflection Rfree: 4056 / Rfactor Rfree: 0.242 / Rfactor Rwork: 0.213
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg27.5
LS refinement shell
*PLUS
Highest resolution: 2.5 Å / Lowest resolution: 2.61 Å / Rfactor Rfree: 0.365 / Rfactor Rwork: 0.285

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