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- PDB-3n8t: Native structure of TK1436, a GH57 branching enzyme from hyperthe... -

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Basic information

Entry
Database: PDB / ID: 3n8t
TitleNative structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis
Componentsalpha-amylase, GH57 family
KeywordsTRANSFERASE / GH57 family member / branching enzyme
Function / homology
Function and homology information


alpha-glucan biosynthetic process / 1,4-alpha-glucan branching enzyme / 1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) / 1,4-alpha-glucan branching enzyme activity / nucleotide binding
Similarity search - Function
1,4-alpha-glucan branching enzyme, C-terminal / Glycoside hydrolase families 57, central domain / 1,4-alpha-glucan branching enzyme MT3115-like / 1,4-alpha-glucan branching enzyme, C-terminal / immunoglobulin/albumin-binding domain-like / Families 57/38 glycoside transferase, middle domain / Glycoside hydrolase family 57, N-terminal domain / Glycosyl hydrolase family 57 / Glycoside hydrolase 38, N terminal domain / 7-stranded beta/alpha barrel ...1,4-alpha-glucan branching enzyme, C-terminal / Glycoside hydrolase families 57, central domain / 1,4-alpha-glucan branching enzyme MT3115-like / 1,4-alpha-glucan branching enzyme, C-terminal / immunoglobulin/albumin-binding domain-like / Families 57/38 glycoside transferase, middle domain / Glycoside hydrolase family 57, N-terminal domain / Glycosyl hydrolase family 57 / Glycoside hydrolase 38, N terminal domain / 7-stranded beta/alpha barrel / Glycoside hydrolase 38, N-terminal domain superfamily / Glycoside hydrolase families 57/38, central domain superfamily / Glycoside hydrolase/deacetylase, beta/alpha-barrel / DNA repair Rad51/transcription factor NusA, alpha-helical / Alpha-Beta Barrel / Up-down Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / 1,4-alpha-glucan branching enzyme TK1436
Similarity search - Component
Biological speciesThermococcus kodakarensis (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsSantos, C.R. / Tonoli, C.C.C. / Trindade, D.M. / Betzel, C. / Takata, H. / Kuriki, T. / Kanai, T. / Imanaka, T. / Arni, R.K. / Murakami, M.T.
CitationJournal: Proteins / Year: 2011
Title: Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1.
Authors: Santos, C.R. / Tonoli, C.C. / Trindade, D.M. / Betzel, C. / Takata, H. / Kuriki, T. / Kanai, T. / Imanaka, T. / Arni, R.K. / Murakami, M.T.
History
DepositionMay 28, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 27, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: alpha-amylase, GH57 family
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,4683
Polymers66,1681
Non-polymers3002
Water4,053225
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)70.424, 78.953, 134.222
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein alpha-amylase, GH57 family /


Mass: 66167.953 Da / Num. of mol.: 1 / Fragment: UNP residues 1-562
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermococcus kodakarensis (archaea) / Strain: KOD1 / Gene: TK1436 / Plasmid: pET21a(+) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIL
References: UniProt: Q5JDJ7, 1,4-alpha-glucan branching enzyme
#2: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#3: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL / Polyethylene glycol


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 225 / 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: 2.82 Å3/Da / Density % sol: 56.38 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 100 mM sodium acetate (pH 5.5), 15% (w/v) PEG 8000, 10% (v/v) PEG 400 and 200 mM sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: LNLS / Beamline: W01B-MX2 / Wavelength: 1.4586 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 10, 2010
RadiationMonochromator: Si (111) double-crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.4586 Å / Relative weight: 1
ReflectionResolution: 2.4→68.1 Å / Num. obs: 29790 / % possible obs: 99.3 % / Redundancy: 4.2 % / Biso Wilson estimate: 46.19 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 12.6
Reflection shellResolution: 2.4→2.49 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.6 / Num. unique all: 2906 / % possible all: 98.7

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
AMoREphasing
REFMAC5.5.0102refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1UFA
Resolution: 2.4→68.05 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.919 / SU B: 6.93 / SU ML: 0.165 / Cross valid method: THROUGHOUT / ESU R Free: 0.245 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24181 1510 5.1 %RANDOM
Rwork0.18148 ---
obs0.18456 28226 99.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 39.958 Å2
Baniso -1Baniso -2Baniso -3
1--0.19 Å20 Å20 Å2
2---0.03 Å20 Å2
3---0.21 Å2
Refinement stepCycle: LAST / Resolution: 2.4→68.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4582 0 20 225 4827
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0224740
X-RAY DIFFRACTIONr_angle_refined_deg1.8061.9486409
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.8125549
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.09923.145248
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.43915810
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.4281539
X-RAY DIFFRACTIONr_chiral_restr0.1280.2645
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0213677
X-RAY DIFFRACTIONr_mcbond_it1.1131.52735
X-RAY DIFFRACTIONr_mcangle_it2.11824412
X-RAY DIFFRACTIONr_scbond_it3.26832005
X-RAY DIFFRACTIONr_scangle_it5.3374.51997
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.306 121 -
Rwork0.236 2012 -
obs--98.7 %

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