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- PDB-1t36: Crystal structure of E. coli carbamoyl phosphate synthetase small... -

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Basic information

Entry
Database: PDB / ID: 1t36
TitleCrystal structure of E. coli carbamoyl phosphate synthetase small subunit mutant C248D complexed with uridine 5'-monophosphate
Components(Carbamoyl-phosphate synthase ...) x 2
KeywordsLIGASE / channeling / pyrimidine biosynthesis / arginine biosynthesis
Function / homology
Function and homology information


carbamoyl-phosphate synthase complex / carbamoyl-phosphate synthase (ammonia) activity / carbamoyl-phosphate synthase (glutamine-hydrolysing) / carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity / pyrimidine nucleobase biosynthetic process / arginine biosynthetic process / glutamine metabolic process / amino acid binding / cellular amino acid biosynthetic process / nitrogen compound metabolic process ...carbamoyl-phosphate synthase complex / carbamoyl-phosphate synthase (ammonia) activity / carbamoyl-phosphate synthase (glutamine-hydrolysing) / carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity / pyrimidine nucleobase biosynthetic process / arginine biosynthetic process / glutamine metabolic process / amino acid binding / cellular amino acid biosynthetic process / nitrogen compound metabolic process / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / nucleotide binding / ATP binding / metal ion binding / cytosol / cytoplasm
Carbamoyl-phosphate synthase small subunit, GATase1 domain / Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily / Pre-ATP-grasp domain superfamily / ATP-grasp fold / Methylglyoxal synthase-like domain / Carbamoyl-phosphate synthase, large subunit / Carbamoyl-phosphate synthase, small subunit / Carbamoyl-phosphate synthase large subunit, CPSase domain / Carbamoyl-phosphate synthetase, large subunit oligomerisation domain / Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain ...Carbamoyl-phosphate synthase small subunit, GATase1 domain / Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily / Pre-ATP-grasp domain superfamily / ATP-grasp fold / Methylglyoxal synthase-like domain / Carbamoyl-phosphate synthase, large subunit / Carbamoyl-phosphate synthase, small subunit / Carbamoyl-phosphate synthase large subunit, CPSase domain / Carbamoyl-phosphate synthetase, large subunit oligomerisation domain / Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain / Carbamoyl-phosphate synthase small subunit, N-terminal domain / Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain / Carbamoyl-phosphate synthase small subunit, N-terminal domain superfamily / Methylglyoxal synthase-like domain superfamily / Class I glutamine amidotransferase-like / MGS-like domain / Carbamoyl-phosphate synthase L chain, ATP binding domain / Carbamoyl-phosphate synthetase large chain, oligomerisation domain / Glutamine amidotransferase class-I / Carbamoyl-phosphate synthase small chain, CPSase domain / Glutamine amidotransferase / Carbamoyl-phosphate synthetase, large subunit oligomerisation domain / Carbamoyl-phosphate synthase small subunit, N-terminal domain / Carbamoyl Phosphate Synthetase; Chain A, domain 4 / Methylglyoxal synthase-like domain / Glucose Oxidase; domain 1 / Rossmann fold - #20 / ATP-grasp fold, A domain / Class I glutamine amidotransferase (GATase) domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / Dna Ligase; domain 1 / 3-Layer(bba) Sandwich / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Carbamoyl-phosphate synthase small chain / Carbamoyl-phosphate synthase large chain / Carbamoyl-phosphate synthase small chain
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.1 Å
AuthorsThoden, J.B. / Huang, X. / Raushel, F.M. / Holden, H.M.
CitationJournal: Protein Sci. / Year: 2004
Title: Long-range allosteric transitions in carbamoyl phosphate synthetase.
Authors: Thoden, J.B. / Huang, X. / Kim, J. / Raushel, F.M. / Holden, H.M.
Validation Report
SummaryFull reportAbout validation report
History
DepositionApr 24, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 21, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Carbamoyl-phosphate synthase large chain
B: Carbamoyl-phosphate synthase small chain
C: Carbamoyl-phosphate synthase large chain
D: Carbamoyl-phosphate synthase small chain
E: Carbamoyl-phosphate synthase large chain
F: Carbamoyl-phosphate synthase small chain
G: Carbamoyl-phosphate synthase large chain
H: Carbamoyl-phosphate synthase small chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)646,61894
Polymers637,9028
Non-polymers8,71586
Water70,3853907
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)152.500, 164.900, 333.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsHetero-octamer comprising chains A,B,C,D,E,F,G,H. THese chains, as deposited, represent the biological assebmly

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Components

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Carbamoyl-phosphate synthase ... , 2 types, 8 molecules ACEGBDFH

#1: Protein
Carbamoyl-phosphate synthase large chain / Carbamoyl-phosphate synthetase ammonia chain


Mass: 117981.750 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: CARB, PYRA, B0033 / Plasmid: pet15 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21
References: UniProt: P00968, carbamoyl-phosphate synthase (glutamine-hydrolysing)
#2: Protein
Carbamoyl-phosphate synthase small chain / Carbamoyl-phosphate synthetase glutamine chain


Mass: 41493.824 Da / Num. of mol.: 4 / Mutation: C248D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: CARA, PYRA, B0032, Z0037, ECS0035 / Plasmid: pet15 / Production host: Escherichia coli (E. coli)
References: UniProt: P00907, UniProt: P0A6F1*PLUS, carbamoyl-phosphate synthase (glutamine-hydrolysing)

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Non-polymers , 9 types, 3993 molecules

#3: Chemical
ChemComp-MN / MANGANESE (II) ION / Manganese


Mass: 54.938 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mn
#4: Chemical...
ChemComp-K / POTASSIUM ION / Potassium


Mass: 39.098 Da / Num. of mol.: 22 / Source method: obtained synthetically / Formula: K
#5: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: PO4
#6: Chemical...
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 27 / Source method: obtained synthetically / Formula: Cl
#7: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#8: Chemical
ChemComp-ORN / L-ornithine / Ornithine


Mass: 132.161 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H12N2O2
#9: Chemical
ChemComp-NET / TETRAETHYLAMMONIUM ION / Tetraethylammonium


Mass: 130.251 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H20N
#10: Chemical
ChemComp-U / URIDINE-5'-MONOPHOSPHATE / Uridine monophosphate


Mass: 324.181 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C9H13N2O9P
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 3907 / 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: 3.2 Å3/Da / Density % sol: 62 %
Crystal growTemperature: 277 K / Method: batch / pH: 7.4
Details: PEG 8000, tetramethylammonium chloride, potassium chloride, manganese chloride, ornithine, ADP, HEPES, pH 7.4, batch, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.65 Å
DetectorType: CUSTOM-MADE / Detector: CCD / Date: Nov 11, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.65 Å / Relative weight: 1
ReflectionResolution: 2.1→30 Å / Num. all: 433843 / Num. obs: 433843 / % possible obs: 90 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rsym value: 0.048 / Net I/σ(I): 15.2
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 2.3 % / Mean I/σ(I) obs: 3.3 / Num. unique all: 39976 / Rsym value: 0.203 / % possible all: 83

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Processing

Software
NameClassification
d*TREKdata scaling
SCALEPACKdata scaling
TNTrefinement
d*TREKdata reduction
TNTphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB entry 1JDB
Resolution: 2.1→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.209 42551 -randon
Rwork0.176 ---
Obs0.179 433843 90 %-
All-433843 --
Refinement stepCycle: LAST / Resolution: 2.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms44228 0 458 3907 48593
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.012
X-RAY DIFFRACTIONt_angle_deg2.43

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