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- PDB-2wl5: BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348N MUTA... -

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Basic information

Entry
Database: PDB / ID: 2wl5
TitleBIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348N MUTANT WITH COENZYME A.
Components(ACETYL-COA ACETYLTRANSFERASE) x 2
KeywordsTRANSFERASE / ACYLTRANSFERASE / CYTOPLASM / PHB BIOSYNTHESIS / THIOLASE FOLD
Function / homology
Function and homology information


poly-hydroxybutyrate biosynthetic process / acetyl-CoA C-acetyltransferase / acetyl-CoA C-acetyltransferase activity / cytoplasm
Similarity search - Function
Thiolase, active site / Thiolases active site. / Thiolase, acyl-enzyme intermediate active site / Thiolases acyl-enzyme intermediate signature. / Thiolase, conserved site / Thiolases signature 2. / Thiolase / Thiolase, C-terminal / Thiolase, C-terminal domain / Thiolase, N-terminal ...Thiolase, active site / Thiolases active site. / Thiolase, acyl-enzyme intermediate active site / Thiolases acyl-enzyme intermediate signature. / Thiolase, conserved site / Thiolases signature 2. / Thiolase / Thiolase, C-terminal / Thiolase, C-terminal domain / Thiolase, N-terminal / Thiolase, N-terminal domain / Thiolase/Chalcone synthase / Peroxisomal Thiolase; Chain A, domain 1 / Thiolase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
COENZYME A / D-mannose / Acetyl-CoA acetyltransferase
Similarity search - Component
Biological speciesZOOGLOEA RAMIGERA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsMerilainen, G. / Poikela, V. / Kursula, P. / Wierenga, R.K.
CitationJournal: Biochemistry / Year: 2009
Title: The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Authors: Merilainen, G. / Poikela, V. / Kursula, P. / Wierenga, R.K.
History
DepositionJun 22, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 3, 2009Provider: repository / Type: Initial release
Revision 1.1Nov 2, 2011Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Refinement description / Version format compliance
Revision 1.2Aug 9, 2017Group: Data collection / Source and taxonomy / Category: diffrn_detector / entity_src_gen
Item: _diffrn_detector.type / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AE" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ACETYL-COA ACETYLTRANSFERASE
B: ACETYL-COA ACETYLTRANSFERASE
C: ACETYL-COA ACETYLTRANSFERASE
D: ACETYL-COA ACETYLTRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)165,76026
Polymers162,1014
Non-polymers3,65922
Water22,1941232
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18190 Å2
ΔGint-176 kcal/mol
Surface area49700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.700, 79.200, 153.000
Angle α, β, γ (deg.)90.00, 92.50, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-1, 0.001437, 0.005592), (-0.001434, -1, 0.000458), (0.005592, 0.00045, 1)42.35, 0.02705, -0.1865
2given(0.4332, -0.8994, -0.05801), (-0.9008, -0.4342, 0.00595), (-0.03054, 0.04968, -0.9983)14.59, 19.37, 68.75
3given(-0.432, 0.8998, -0.06063), (0.9015, 0.4329, 0.001651), (0.02773, -0.05395, -0.9982)32.9, -18.84, 67.62

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein ACETYL-COA ACETYLTRANSFERASE / ACETOACETYL-COA THIOLASE


Mass: 40533.168 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-11,12-392 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: SUBUNITS A AND B COMPLEXED WITH COA / Source: (gene. exp.) ZOOGLOEA RAMIGERA (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P07097, acetyl-CoA C-acetyltransferase
#2: Protein ACETYL-COA ACETYLTRANSFERASE / ACETOACETYL-COA THIOLASE


Mass: 40517.164 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-11,12-392
Source method: isolated from a genetically manipulated source
Details: SUBUNITS A AND B COMPLEXED WITH COA / Source: (gene. exp.) ZOOGLOEA RAMIGERA (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P07097, acetyl-CoA C-acetyltransferase

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Sugars , 1 types, 4 molecules

#4: Sugar
ChemComp-DNO / D-mannose / Mannose


Type: D-saccharide / Mass: 180.156 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C6H12O6

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Non-polymers , 5 types, 1250 molecules

#3: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-COA / COENZYME A / Coenzyme A


Mass: 767.534 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#7: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1232 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, HIS 348 TO ASN ENGINEERED RESIDUE IN CHAIN B, HIS 348 TO ASN ...ENGINEERED RESIDUE IN CHAIN A, HIS 348 TO ASN ENGINEERED RESIDUE IN CHAIN B, HIS 348 TO ASN ENGINEERED RESIDUE IN CHAIN C, HIS 348 TO ASN ENGINEERED RESIDUE IN CHAIN D, HIS 348 TO ASN
Nonpolymer detailsCOENZYME A (COA): COENZYME A IS BOUND IN SUBUNITS A AND B.
Sequence detailsA11 INSERTION AND A129R MUTATION WERE FOUND TO EXIST IN THE WILD TYPE CLONE USED AND IS ALREADY ...A11 INSERTION AND A129R MUTATION WERE FOUND TO EXIST IN THE WILD TYPE CLONE USED AND IS ALREADY DESCRIBED IN THE FIRST STRUCTURE PUBLISHED FROM THIS ENZYME, IN THE ARTICLE (STRUCTURE 1999, 7:1279-1290)

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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: 3.2 Å3/Da / Density % sol: 62 % / Description: NONE
Crystal growpH: 5.5
Details: 0.75 M LI2SO4, 1.7 M (NH4)2SO4, 0.1 M SODIUM CITRATE (PH 5.5), 1 MM EDTA, 1 MM NAN3 AND 1 MM DTT

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9334
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 27, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9334 Å / Relative weight: 1
ReflectionResolution: 1.8→20 Å / Num. obs: 184515 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 19.8 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.1
Reflection shellResolution: 1.8→1.95 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 3.2 / % possible all: 99.5

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1DLU

1dlu


Resolution: 1.8→19.388 Å / SU ML: 0.54 / σ(F): 2 / Phase error: 20.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2566 9226 5 %
Rwork0.2209 --
obs0.2227 184508 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 81.964 Å2 / ksol: 0.463 e/Å3
Displacement parametersBiso mean: 36.8 Å2
Baniso -1Baniso -2Baniso -3
1--5.6291 Å20 Å20.1534 Å2
2---4.7735 Å20 Å2
3----4.5464 Å2
Refinement stepCycle: LAST / Resolution: 1.8→19.388 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11246 0 216 1232 12694
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00911708
X-RAY DIFFRACTIONf_angle_d1.13515856
X-RAY DIFFRACTIONf_dihedral_angle_d17.3814366
X-RAY DIFFRACTIONf_chiral_restr0.0771760
X-RAY DIFFRACTIONf_plane_restr0.0062076
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.82050.27552960.24765618X-RAY DIFFRACTION96
1.8205-1.84190.29783020.2465737X-RAY DIFFRACTION97
1.8419-1.86430.25882990.22845696X-RAY DIFFRACTION97
1.8643-1.88790.24723040.21915759X-RAY DIFFRACTION97
1.8879-1.91270.2573010.21235733X-RAY DIFFRACTION97
1.9127-1.93890.2433040.20355771X-RAY DIFFRACTION98
1.9389-1.96660.23173050.19485793X-RAY DIFFRACTION98
1.9666-1.99590.24443030.20245763X-RAY DIFFRACTION98
1.9959-2.0270.26673070.20655830X-RAY DIFFRACTION98
2.027-2.06020.23883030.19695751X-RAY DIFFRACTION98
2.0602-2.09570.22833090.19065872X-RAY DIFFRACTION99
2.0957-2.13380.23583060.19295815X-RAY DIFFRACTION99
2.1338-2.17480.22683090.19385865X-RAY DIFFRACTION99
2.1748-2.21910.21143070.18615850X-RAY DIFFRACTION99
2.2191-2.26730.23733090.1845868X-RAY DIFFRACTION99
2.2673-2.31990.2383100.18895893X-RAY DIFFRACTION99
2.3199-2.37790.23653080.18835839X-RAY DIFFRACTION100
2.3779-2.4420.21873090.19025880X-RAY DIFFRACTION100
2.442-2.51380.23853120.1975922X-RAY DIFFRACTION100
2.5138-2.59470.25653110.20545912X-RAY DIFFRACTION100
2.5947-2.68720.25543110.20815915X-RAY DIFFRACTION100
2.6872-2.79450.23383090.20415871X-RAY DIFFRACTION100
2.7945-2.92130.26083120.21185926X-RAY DIFFRACTION99
2.9213-3.07470.26543100.21795886X-RAY DIFFRACTION99
3.0747-3.26650.25673090.21575869X-RAY DIFFRACTION99
3.2665-3.51740.23623110.20775904X-RAY DIFFRACTION99
3.5174-3.86880.22353110.20915905X-RAY DIFFRACTION99
3.8688-4.42280.22723120.20885939X-RAY DIFFRACTION99
4.4228-5.55050.26113130.23775939X-RAY DIFFRACTION99
5.5505-19.38910.33543140.29825961X-RAY DIFFRACTION97
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.1868-0.1665-0.04570.3103-0.0970.0606-0.0346-0.0043-0.01710.01550.0343-0.0196-0.0195-0.00760.00220.00050.0022-0.00180.00650.00110.015430.7025-12.39837.0361
20.1561-0.18920.05090.28660.0440.0428-0.0247-0.0130.0160.01110.02510.01040.01650.0133-0.00310.0053-0.00240.00460.0139-0.00280.000911.701912.32736.9358
30.22020.0250.12580.64180.04450.12980.0455-0.0668-0.01830.5855-0.0141-0.2554-0.0846-0.0353-0.02060.49720.0735-0.21030.19090.0080.185238.5414-2.807660.1782
40.3060.0809-0.06430.7007-0.13110.0308-0.0317-0.22570.04580.6584-0.0010.1989-0.0466-0.0056-0.0340.53650.13280.13120.2272-0.02270.05388.14833.421562.1012
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A
2X-RAY DIFFRACTION2CHAIN B
3X-RAY DIFFRACTION3CHAIN C
4X-RAY DIFFRACTION4CHAIN D

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