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- PDB-5b0k: Structure of MoeN5-Sso7d fusion protein in complex with beta-decy... -

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Basic information

Entry
Database: PDB / ID: 5b0k
TitleStructure of MoeN5-Sso7d fusion protein in complex with beta-decyl maltoside
ComponentsMoeN5,DNA-binding protein 7d
KeywordsTRANSFERASE / DNA BINDING PROTEIN / prenyltransferase / alpha-helical fold / complex / fusion tag
Function / homology
Function and homology information


RNA endonuclease activity / DNA binding / cytoplasm
Similarity search - Function
DNA-binding 7kDa protein / 7kD DNA-binding domain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #40 / Chromo-like domain superfamily / Farnesyl Diphosphate Synthase / Farnesyl Diphosphate Synthase / Isoprenoid synthase domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Orthogonal Bundle ...DNA-binding 7kDa protein / 7kD DNA-binding domain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #40 / Chromo-like domain superfamily / Farnesyl Diphosphate Synthase / Farnesyl Diphosphate Synthase / Isoprenoid synthase domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
MoeN5 / DNA-binding protein 7d
Similarity search - Component
Biological speciesStreptomyces ghanaensis (bacteria)
Sulfolobus solfataricus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.75 Å
AuthorsKo, T.-P. / Zhang, L. / Chen, C.-C. / Guo, R.-T.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2016
Title: Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.
Authors: Zhang, L. / Chen, C.C. / Ko, T.P. / Huang, J.W. / Zheng, Y. / Liu, W. / Wang, I. / Malwal, S.R. / Feng, X. / Wang, K. / Huang, C.H. / Hsu, S.T. / Wang, A.H. / Oldfield, E. / Guo, R.T.
History
DepositionOct 30, 2015Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 23, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 20, 2016Group: Database references
Revision 1.2Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MoeN5,DNA-binding protein 7d
B: MoeN5,DNA-binding protein 7d
C: MoeN5,DNA-binding protein 7d
D: MoeN5,DNA-binding protein 7d
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,22210
Polymers150,3274
Non-polymers2,8956
Water12,647702
1
A: MoeN5,DNA-binding protein 7d
B: MoeN5,DNA-binding protein 7d
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,0946
Polymers75,1642
Non-polymers1,9304
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7770 Å2
ΔGint-50 kcal/mol
Surface area24430 Å2
MethodPISA
2
C: MoeN5,DNA-binding protein 7d
D: MoeN5,DNA-binding protein 7d
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,1294
Polymers75,1642
Non-polymers9652
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5900 Å2
ΔGint-40 kcal/mol
Surface area23850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)137.448, 219.649, 104.185
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number21
Space group name H-MC222
Components on special symmetry positions
IDModelComponents
11A-677-

HOH

21A-733-

HOH

31A-737-

HOH

41A-758-

HOH

51B-742-

HOH

61C-580-

HOH

71D-639-

HOH

81D-660-

HOH

91D-675-

HOH

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Components

#1: Protein
MoeN5,DNA-binding protein 7d / prenyltransferase / 7 kDa DNA-binding protein d / Sso7d


Mass: 37581.781 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: The fusion protein of prenyltransferase (RESIDUES 1-260), LINKER AGAGA (RESIDUES 261-265) and Sso7d (RESIDUES 266-329)
Source: (gene. exp.) Streptomyces ghanaensis (bacteria), (gene. exp.) Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (archaea)
Gene: moeN5, sso7d, sso7d-1, SSO10610 / Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A010, UniProt: P39476
#2: Sugar
ChemComp-DMU / DECYL-BETA-D-MALTOPYRANOSIDE / DECYLMALTOSIDE


Type: D-saccharide / Mass: 482.562 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C22H42O11 / Comment: detergent*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 702 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.62 Å3/Da / Density % sol: 52.97 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.1
Details: 0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350, 5% glycerol, 1% beta-decyl-D-maltoside

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 14, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.75→25 Å / Num. obs: 41493 / % possible obs: 98.4 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 12.4
Reflection shellResolution: 2.75→2.85 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.442 / Mean I/σ(I) obs: 2.2 / % possible all: 99.4

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Processing

Software
NameClassification
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing
Blu-Icedata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5B02

5b02


Resolution: 2.75→25 Å / Cross valid method: THROUGHOUT
RfactorNum. reflection% reflectionSelection details
Rfree0.248 1946 4.7 %Random selection
Rwork0.182 ---
obs-38776 93.9 %-
Refine analyzeLuzzati coordinate error obs: 0.29 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.37 Å
Refinement stepCycle: LAST / Resolution: 2.75→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9069 0 198 702 9969

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