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- PDB-1scu: THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA... -

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Basic information

Entry
Database: PDB / ID: 1scu
TitleTHE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION
Components
  • SUCCINYL-COA SYNTHETASE, ALPHA SUBUNITSuccinyl coenzyme A synthetase
  • SUCCINYL-COA SYNTHETASE, BETA SUBUNITSuccinyl coenzyme A synthetase
KeywordsLIGASE (ATP-BINDING)
Function / homology
Function and homology information


succinate-CoA ligase complex / succinate-CoA ligase complex (ADP-forming) / succinate-CoA ligase (GDP-forming) activity / succinyl-CoA metabolic process / succinate-CoA ligase (ADP-forming) / succinate-CoA ligase (ADP-forming) activity / tricarboxylic acid cycle / protein autophosphorylation / nucleotide binding / magnesium ion binding ...succinate-CoA ligase complex / succinate-CoA ligase complex (ADP-forming) / succinate-CoA ligase (GDP-forming) activity / succinyl-CoA metabolic process / succinate-CoA ligase (ADP-forming) / succinate-CoA ligase (ADP-forming) activity / tricarboxylic acid cycle / protein autophosphorylation / nucleotide binding / magnesium ion binding / ATP binding / cytosol / cytoplasm
Similarity search - Function
Succinyl-CoA ligase, alpha subunit / Succinate--CoA synthetase, beta subunit / ATP-grasp domain / ATP-grasp fold, succinyl-CoA synthetase-type / Succinyl-CoA synthetase domains / ATP-citrate lyase/succinyl-CoA ligase, conserved site / ATP-citrate lyase / succinyl-CoA ligases family active site. / ATP-citrate lyase/succinyl-CoA ligase, active site / ATP-citrate lyase / succinyl-CoA ligases family signature 1. / ATP-citrate lyase / succinyl-CoA ligases family signature 3. ...Succinyl-CoA ligase, alpha subunit / Succinate--CoA synthetase, beta subunit / ATP-grasp domain / ATP-grasp fold, succinyl-CoA synthetase-type / Succinyl-CoA synthetase domains / ATP-citrate lyase/succinyl-CoA ligase, conserved site / ATP-citrate lyase / succinyl-CoA ligases family active site. / ATP-citrate lyase/succinyl-CoA ligase, active site / ATP-citrate lyase / succinyl-CoA ligases family signature 1. / ATP-citrate lyase / succinyl-CoA ligases family signature 3. / Succinyl-CoA synthetase, beta subunit, conserved site / CoA-ligase / ATP-citrate lyase/succinyl-CoA ligase / CoA binding domain / Succinyl-CoA synthetase-like / CoA binding domain / CoA-binding / ATP-grasp fold, A domain / ATP-grasp fold, subdomain 1 / ATP-grasp fold profile. / ATP-grasp fold / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / Dna Ligase; domain 1 / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Succinate--CoA ligase [ADP-forming] subunit beta / COENZYME A / Succinate--CoA ligase [ADP-forming] subunit alpha / Succinate--CoA ligase [ADP-forming] subunit alpha
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / Resolution: 2.5 Å
AuthorsWolodko, W.T. / Fraser, M.E. / James, M.N.G. / Bridger, W.A.
Citation
Journal: J.Biol.Chem. / Year: 1994
Title: The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.
Authors: Wolodko, W.T. / Fraser, M.E. / James, M.N. / Bridger, W.A.
#1: Journal: J.Biol.Chem. / Year: 1984
Title: Crystallization of Succinyl-Coa Synthetase from Escherichia Coli
Authors: Wolodko, W.T. / James, M.N.G. / Bridger, W.A.
History
DepositionNov 18, 1993Processing site: BNL
Revision 1.0Apr 20, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 17, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Refinement description
Category: pdbx_database_status / software / struct_conn
Item: _pdbx_database_status.process_site / _software.classification / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Aug 14, 2019Group: Data collection / Refinement description / Category: software / Item: _software.classification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT
B: SUCCINYL-COA SYNTHETASE, BETA SUBUNIT
D: SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT
E: SUCCINYL-COA SYNTHETASE, BETA SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,9286
Polymers142,3934
Non-polymers1,5352
Water1,982110
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)98.470, 98.470, 400.600
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number95
Space group name H-MP4322
Atom site foot note1: CIS PROLINE - PRO A 121 / 2: CIS PROLINE - PRO B 42 / 3: CIS PROLINE - PRO B 200 / 4: CIS PROLINE - PRO D 121 / 5: CIS PROLINE - PRO E 42 / 6: CIS PROLINE - PRO E 200
7: RESIDUE 246 OF EACH ALPHA SUBUNIT IS A PHOSPHORYLATED HISTIDINE.

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Components

#1: Protein SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT / Succinyl coenzyme A synthetase


Mass: 29758.213 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
References: UniProt: P07459, UniProt: P0AGE9*PLUS, succinate-CoA ligase (ADP-forming)
#2: Protein SUCCINYL-COA SYNTHETASE, BETA SUBUNIT / Succinyl coenzyme A synthetase


Mass: 41438.496 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
References: UniProt: P0A836, succinate-CoA ligase (ADP-forming)
#3: Chemical ChemComp-COA / COENZYME A / Coenzyme A


Mass: 767.534 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 110 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsAMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT THE FIRST RESIDUE IS A SERINE (W. A. ...AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT THE FIRST RESIDUE IS A SERINE (W. A. BRIDGE, ENZYMES, 3RD ED. 10, 581-606 (1974)). IN THE GENE SEQUENCING PAPER, BUCK, SPENCER AND GUEST STATE THAT "[THE ASSUMPTION IS] THAT THE INITIATING FORMYLMETHIONINE IS REMOVED POSTTRANSLATIONALLY FROM THE ALPHA BUT NOT FROM THE BETA SUBUNIT" (D. BUCK, M. E. SPENCER, AND J. R. GUEST, BIOCHEMISTRY 24, 6245-6252 (1985)).

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.41 Å3/Da / Density % sol: 63.93 %
Crystal grow
*PLUS
Temperature: 21 ℃ / pH: 7.3 / Method: microdialysis / Details: Wolodko, W.T., (1984) J. Biol. Chem., 259, 5316.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
110 mg/mlenzyme11
21.9 Mammonium sulfate12
30.1 Mpotassium phosphate12
41 mMdithiothreitol12
50.1 mMCoA12
60.1 mMEDTA12

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

Software
NameClassification
X-PLORmodel building
TNTrefinement
X-PLORrefinement
X-PLORphasing
RefinementResolution: 2.5→100 Å / σ(F): 0 /
RfactorNum. reflection
Rwork0.216 -
obs0.216 67272
Refinement stepCycle: LAST / Resolution: 2.5→100 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9982 0 96 110 10188
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.022
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg3.25
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it

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