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- PDB-2hg8: Crystal Structure of Cys315Ala mutant of human mitochondrial bran... -

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Basic information

Entry
Database: PDB / ID: 2hg8
TitleCrystal Structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase complexed with its substrate mimic, N-methyl leucine.
ComponentsBranched-chain-amino-acid aminotransferase, mitochondrial
KeywordsTRANSFERASE / D-aminoacid aminotransferase-like PLP-dependent enzymes
Function / homology
Function and homology information


regulation of hormone levels / branched-chain-amino-acid transaminase activity / isoleucine catabolic process / L-leucine:2-oxoglutarate aminotransferase activity / branched-chain-amino-acid transaminase / L-leucine transaminase activity / L-valine transaminase activity / L-isoleucine transaminase activity / branched-chain amino acid biosynthetic process / Branched-chain amino acid catabolism ...regulation of hormone levels / branched-chain-amino-acid transaminase activity / isoleucine catabolic process / L-leucine:2-oxoglutarate aminotransferase activity / branched-chain-amino-acid transaminase / L-leucine transaminase activity / L-valine transaminase activity / L-isoleucine transaminase activity / branched-chain amino acid biosynthetic process / Branched-chain amino acid catabolism / L-leucine biosynthetic process / valine biosynthetic process / cellular response to leukemia inhibitory factor / lipid metabolic process / mitochondrial matrix / mitochondrion / nucleoplasm
Similarity search - Function
Branched-chain amino acid aminotransferase II / Branched-chain aminotransferase / Aminotransferase, class IV, conserved site / Aminotransferases class-IV signature. / Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain / D-amino Acid Aminotransferase; Chain A, domain 2 / D-amino Acid Aminotransferase, subunit A, domain 2 / Aminotransferase class IV / Aminotransferase-like, PLP-dependent enzymes / Branched-chain-amino-acid aminotransferase-like, N-terminal ...Branched-chain amino acid aminotransferase II / Branched-chain aminotransferase / Aminotransferase, class IV, conserved site / Aminotransferases class-IV signature. / Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain / D-amino Acid Aminotransferase; Chain A, domain 2 / D-amino Acid Aminotransferase, subunit A, domain 2 / Aminotransferase class IV / Aminotransferase-like, PLP-dependent enzymes / Branched-chain-amino-acid aminotransferase-like, N-terminal / Branched-chain-amino-acid aminotransferase-like, C-terminal / Amino-transferase class IV / D-amino Acid Aminotransferase; Chain A, domain 1 / Alpha-Beta Barrel / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETIC ACID / N-METHYLLEUCINE / PYRIDOXAL-5'-PHOSPHATE / Branched-chain-amino-acid aminotransferase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsYennawar, N.H. / Hutson, S.M.
Citation
Journal: J.Biol.Chem. / Year: 2006
Title: Human Mitochondrial Branched Chain Aminotransferase Isozyme: STRUCTURAL ROLE OF THE CXXC CENTER IN CATALYSIS.
Authors: Yennawar, N.H. / Islam, M.M. / Conway, M. / Wallin, R. / Hutson, S.M.
#1: Journal: J.BIOL.CHEM. / Year: 1998
Title: Overexpression and characterization of the human mitochondrial and cytosolic branched-chain aminotransferases.
Authors: Davoodi, J. / Drown, P.M. / Bledsoe, R.K. / Wallin, R. / Reinhart, G.D. / Hutson, S.M.
#2: Journal: Biochim.Biophys.Acta / Year: 1997
Title: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm).
Authors: Bledsoe, R.K. / Dawson, P.A. / Hutson, S.M.
History
DepositionJun 26, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 24, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Oct 18, 2017Group: Advisory / Refinement description / Category: pdbx_unobs_or_zero_occ_atoms / software
Revision 1.4Oct 20, 2021Group: Advisory / Database references / Derived calculations
Category: database_2 / pdbx_unobs_or_zero_occ_atoms ...database_2 / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Branched-chain-amino-acid aminotransferase, mitochondrial
B: Branched-chain-amino-acid aminotransferase, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,5177
Polymers82,6722
Non-polymers8455
Water6,071337
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6750 Å2
ΔGint-37 kcal/mol
Surface area28210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.179, 109.278, 59.449
Angle α, β, γ (deg.)90.000, 97.230, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Branched-chain-amino-acid aminotransferase, mitochondrial / BCATm / Placental protein 18 / PP18 / Mitochondrial Branched Chain Aminotransferase


Mass: 41335.953 Da / Num. of mol.: 2 / Mutation: C315A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BCAT2, BCATM, ECA40 / Plasmid: PET-28A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Bl21de3
References: UniProt: O15382, branched-chain-amino-acid transaminase
#2: Chemical ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate / Pyridoxal phosphate


Mass: 247.142 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H10NO6P
#3: Chemical ChemComp-MLE / N-METHYLLEUCINE


Type: L-peptide linking / Mass: 145.199 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H15NO2
#4: Chemical ChemComp-ACY / ACETIC ACID / Acetic acid


Mass: 60.052 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H4O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 337 / 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: 2.31 Å3/Da / Density % sol: 46.64 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7
Details: PEG1500, HEPES, DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.91609 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 1, 2002 / Details: Si(111)
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91609 Å / Relative weight: 1
ReflectionResolution: 1.8→30 Å / Num. all: 69464 / Num. obs: 64199 / % possible obs: 92.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.074 / Χ2: 1.057 / Net I/σ(I): 16.7
Reflection shell
Resolution (Å)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.8-1.830.21432011.018192.8
1.83-1.860.21132811.069194.4
1.86-1.90.17832671.036195.6
1.9-1.940.1533481.021196.3
1.94-1.980.13733141.052196
1.98-2.030.12233351.045196.7
2.03-2.080.11133821.027196.9
2.08-2.130.10433751.039197.3
2.13-2.20.09533821.053197.8
2.2-2.270.08933821.023197.9
2.27-2.350.08433931.098197.8
2.35-2.440.08134081.098198
2.44-2.550.07633661.072197.7
2.55-2.690.07334041.095196.8
2.69-2.860.0733111.065196.2
2.86-3.080.06732461.088193.7
3.08-3.390.06630361.086187.3
3.39-3.880.06526851.039176.4
3.88-4.880.0623381.07166.9
4.88-300.05127451.05177.3

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
PDB_EXTRACT2data extraction
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→25 Å / FOM work R set: 0.799 / σ(F): 0 / Stereochemistry target values: Engh & Huber
Details: Due to a feature in the refinement program, the structure was refined with OXT on one or more residues that is not the terminal residue of the sequence. In all these instances the OXT was ...Details: Due to a feature in the refinement program, the structure was refined with OXT on one or more residues that is not the terminal residue of the sequence. In all these instances the OXT was changed to N of the next residue.
RfactorNum. reflection% reflectionSelection details
Rfree0.282 3166 4.6 %RANDOM
Rwork0.252 ---
all0.252 69464 --
obs0.252 64056 92.5 %-
Solvent computationBsol: 23.066 Å2
Displacement parametersBiso mean: 25.604 Å2
Baniso -1Baniso -2Baniso -3
1-1.039 Å20 Å21.274 Å2
2--4.506 Å20 Å2
3----5.545 Å2
Refinement stepCycle: LAST / Resolution: 1.8→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5740 0 54 337 6131
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.012
X-RAY DIFFRACTIONc_angle_deg1.578
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 50

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection obs
1.8-1.810.294540.30411751229
1.81-1.820.309680.30412501318
1.82-1.840.284780.29211851263
1.84-1.850.284590.27612941353
1.85-1.860.371540.28512311285
1.86-1.880.319570.28512741331
1.88-1.890.332610.29112461307
1.89-1.910.372530.27912821335
1.91-1.920.345660.26612461312
1.92-1.940.309710.26412721343
1.94-1.960.3630.2712621325
1.96-1.970.318860.26212681354
1.97-1.990.241760.25412391315
1.99-2.010.305690.24912671336
2.01-2.030.3660.2512511317
2.03-2.050.247810.24812751356
2.05-2.070.312770.25312571334
2.07-2.090.309770.25812411318
2.09-2.110.308740.24713281402
2.11-2.130.255500.23912801330
2.13-2.160.288680.24912481316
2.16-2.180.273640.25113241388
2.18-2.210.226690.24112611330
2.21-2.240.277670.24512961363
2.24-2.270.293630.24412961359
2.27-2.30.315770.26212711348
2.3-2.330.262580.24412671325
2.33-2.370.282660.24913171383
2.37-2.40.272730.24612751348
2.4-2.440.253640.24212981362
2.44-2.480.301590.2513371396
2.48-2.530.24590.24412571316
2.53-2.580.273850.2412751360
2.58-2.630.295500.24312591309
2.63-2.690.313690.27113111380
2.69-2.750.322660.25912261292
2.75-2.820.271770.26112951372
2.82-2.90.327630.26312381301
2.9-2.980.343430.26512911334
2.98-3.080.26520.24311951247
3.08-3.190.289640.2612061270
3.19-3.310.244740.25311181192
3.31-3.460.286710.25410601131
3.46-3.650.262380.25810191057
3.65-3.870.319510.2610041055
3.87-4.170.284360.246918954
4.17-4.590.17320.227879911
4.59-5.250.302540.2269521006
5.25-6.590.289590.23811571216
6.59-250.218550.232917972
Xplor file
Refine-IDSerial noParam file
X-RAY DIFFRACTION1protein.param
X-RAY DIFFRACTION2water_rep.param
X-RAY DIFFRACTION3acy+glyc.par
X-RAY DIFFRACTION41ML_par.txt

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