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- PDB-2shk: THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA ... -

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Basic information

Entry
Database: PDB / ID: 2shk
TitleTHE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI COMPLEXED WITH ADP
ComponentsSHIKIMATE KINASE
KeywordsTRANSFERASE / SHIKIMATE KINASE / PHOSPHORYL TRANSFER / ADP / SHIKIMATE PATHWAY / P-LOOP PROTEIN
Function / homology
Function and homology information


shikimate kinase / shikimate kinase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / phosphorylation / magnesium ion binding / ATP binding / cytosol
Similarity search - Function
Shikimate kinase 2 / Shikimate kinase, conserved site / Shikimate kinase signature. / Shikimate kinase/Threonine synthase-like 1 / Shikimate kinase/gluconokinase / Shikimate kinase / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Shikimate kinase 2
Similarity search - Component
Biological speciesErwinia chrysanthemi (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.6 Å
AuthorsKrell, T. / Coggins, J.R. / Lapthorn, A.J.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 1997
Title: Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi.
Authors: Krell, T. / Coyle, J.E. / Horsburgh, M.J. / Coggins, J.R. / Lapthorn, A.J.
#1: Journal: J.Mol.Biol. / Year: 1998
Title: The Three-Dimensional Structure of Shikimate Kinase
Authors: Krell, T. / Coggins, J.R. / Lapthorn, A.J.
History
DepositionOct 27, 1997Processing site: BNL
Revision 1.0Nov 18, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: SHIKIMATE KINASE
B: SHIKIMATE KINASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4767
Polymers37,9522
Non-polymers5245
Water2,756153
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1700 Å2
ΔGint-34 kcal/mol
Surface area15430 Å2
MethodPISA
2
B: SHIKIMATE KINASE
hetero molecules

A: SHIKIMATE KINASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,4767
Polymers37,9522
Non-polymers5245
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_545-y+1/2,x-1/2,z+1/41
Buried area2850 Å2
ΔGint-40 kcal/mol
Surface area14270 Å2
MethodPISA
Unit cell
Length a, b, c (Å)108.500, 108.500, 92.800
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (-0.50361, -0.85848, 0.096889), (-0.863822, 0.502148, -0.040719), (-0.013696, -0.104202, -0.994462)
Vector: 80.8699, 48.1827, 30.6194)

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Components

#1: Protein SHIKIMATE KINASE /


Mass: 18975.754 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Erwinia chrysanthemi (bacteria) / Genus: Dickeya / Strain: NCPPB 1066 / Cellular location: CYTOPLASM / Gene: AROL / Plasmid: PTB361SK / Gene (production host): AROL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): (DE3) PLYSS / References: UniProt: P10880, shikimate kinase
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 153 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHE GAP IN THE MOLECULAR STRUCTURE CORRESPONDS TO RESIDUES OF THE LID-DOMAIN. BY ANALOGY TO ...THE GAP IN THE MOLECULAR STRUCTURE CORRESPONDS TO RESIDUES OF THE LID-DOMAIN. BY ANALOGY TO ADENYLATE KINASES THE LID DOMAIN CLOSES OVER BOUND ATP.

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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: 3.6 Å3/Da / Density % sol: 66 %
Crystal growpH: 7.1
Details: 2.16M NACL, 100MM HEPES BUFFER PH 7.1, 5MM ADP, 5MM SHIKIMATE, 10MM MGCL2
Crystal grow
*PLUS
pH: 7.6 / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
120 mMTris-HCl1drop
25 mMADP1drop
310 mM1dropMgCl2
416 mg/mlenzyme1drop
52.16 M1reservoirNaCl
6100 mMHEPES1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX9.5 / Wavelength: 0.92
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1995 / Details: MIRROR
RadiationMonochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 2.6→28 Å / Num. obs: 17402 / % possible obs: 98.8 % / Observed criterion σ(I): 0 / Redundancy: 6.3 % / Rmerge(I) obs: 0.107 / Rsym value: 0.107 / Net I/σ(I): 10
Reflection shellResolution: 2.6→2.69 Å / Redundancy: 5 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 2 / Rsym value: 0.65 / % possible all: 97

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
SHELX-90model building
SHELX-90refinement
SHELX-90phasing
RefinementMethod to determine structure: MIRAS / Resolution: 2.6→20 Å / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.263 1679 10 %RANDOM
Rwork0.186 ---
obs0.184 16862 98.8 %-
Refinement stepCycle: LAST / Resolution: 2.6→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2494 0 31 153 2678

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