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- PDB-1uu0: Histidinol-phosphate aminotransferase (HisC) from Thermotoga mari... -

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Basic information

Entry
Database: PDB / ID: 1uu0
TitleHistidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)
ComponentsHISTIDINOL-PHOSPHATE AMINOTRANSFERASE
KeywordsTRANSFERASE / HISTIDINE BIOSYNTHESIS / AMINOTRANSFERASE / PYRIDOXAL PHOSPHATE
Function / homology
Function and homology information


histidinol-phosphate transaminase / histidinol-phosphate transaminase activity / L-histidine biosynthetic process / pyridoxal phosphate binding / protein homodimerization activity
Similarity search - Function
: / Histidinol-phosphate aminotransferase family / Aminotransferase, class-II, pyridoxal-phosphate binding site / Aminotransferases class-II pyridoxal-phosphate attachment site. / Aminotransferase, class I/classII / Aminotransferase class I and II / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) ...: / Histidinol-phosphate aminotransferase family / Aminotransferase, class-II, pyridoxal-phosphate binding site / Aminotransferases class-II pyridoxal-phosphate attachment site. / Aminotransferase, class I/classII / Aminotransferase class I and II / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Histidinol-phosphate aminotransferase
Similarity search - Component
Biological speciesTHERMOTOGA MARITIMA (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å
AuthorsVega, M.C. / Fernandez, F.J. / Lehmann, F. / Wilmanns, M.
Citation
Journal: J.Biol.Chem. / Year: 2004
Title: Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-Phosphate Aminotransferase
Authors: Fernandez, F.J. / Vega, M.C. / Lehmann, F. / Sandmeier, E. / Gehring, H. / Christen, P. / Wilmanns, M.
#1: Journal: J.Mol.Biol. / Year: 2001
Title: Crystal Structure of Histidinol Phosphate Aminotransferase (Hisc) from Escherichia Coli, and its Covalent Complex with Pyridoxal-5'-Phosphate and L-Histidinol Phosphate
Authors: Sivaraman, J. / Li, Y. / Larocque, R. / Schrag, J.D. / Cygler, M. / Matte, A.
History
DepositionDec 12, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 13, 2004Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 24, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
B: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
C: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
D: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)157,7848
Polymers157,4044
Non-polymers3804
Water1,964109
1
A: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
B: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,8924
Polymers78,7022
Non-polymers1902
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
C: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
D: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,8924
Polymers78,7022
Non-polymers1902
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)183.826, 139.800, 53.409
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
HISTIDINOL-PHOSPHATE AMINOTRANSFERASE / IMIDAZOLE ACETOL-PHOSPHATE TRANAMINASE / HISC


Mass: 39350.945 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: PHOSPHATE ANION ATTACHED PER CHAIN / Source: (gene. exp.) THERMOTOGA MARITIMA (bacteria) / Plasmid: PETM11 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q9X0D0, histidinol-phosphate transaminase
#2: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 109 / Source method: isolated from a natural source / Formula: H2O
Compound detailsCATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE = 3- (IMIDAZOL-4-YL)-2-OXOPROPYL ...CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE = 3- (IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + L-GLUTAMATE.

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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: 2.4 Å3/Da / Density % sol: 44.7 %
Crystal growpH: 7 / Details: pH 7.00

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8416
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8416 Å / Relative weight: 1
ReflectionResolution: 2.85→20 Å / Num. obs: 31839 / % possible obs: 95 % / Redundancy: 2.5 % / Biso Wilson estimate: 45.8 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 13.5
Reflection shellResolution: 2.85→2.95 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.294 / Mean I/σ(I) obs: 3.6 / % possible all: 97.9

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Processing

Software
NameVersionClassification
CNS1.1refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1H1C

1h1c


Resolution: 2.85→24.11 Å / Rfactor Rfree error: 0.005 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.284 2915 10 %RANDOM
Rwork0.221 ---
obs0.221 29180 88.4 %-
Solvent computationSolvent model: FLAT MODEL / ksol: 0.25071 e/Å3
Displacement parametersBiso mean: 48.1 Å2
Baniso -1Baniso -2Baniso -3
1--3.1 Å20 Å20 Å2
2--9.85 Å20 Å2
3----6.75 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.52 Å0.36 Å
Luzzati d res low-5 Å
Luzzati sigma a0.59 Å0.39 Å
Refinement stepCycle: LAST / Resolution: 2.85→24.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10623 0 20 109 10752
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.004
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.2
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d22.3
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.69
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 2.85→3.03 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.363 567 10.7 %
Rwork0.282 4741 -
obs--98.2 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION3ION.PARAMION.TOP

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