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- SASDD32: DNA-(adenine N6)-methyltransferase from Acinetobacter baumannii A... -

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Entry
Database: SASBDB / ID: SASDD32
SampleDNA-(adenine N6)-methyltransferase from Acinetobacter baumannii ATCC 17978
  • DNA-(adenine N6)-methyltransferase (protein), A1S_0222, Acinetobacter baumannii ATCC 17978
Biological speciesAcinetobacter baumannii ATCC 17978 (bacteria)
CitationJournal: Protein Expr Purif / Year: 2018
Title: Recombinant production of A1S_0222 from Acinetobacter baumannii ATCC 17978 and confirmation of its DNA-(adenine N6)-methyltransferase activity.
Authors: Ulrike Blaschke / Beneditta Suwono / Sachli Zafari / Ingo Ebersberger / Evelyn Skiebe / Cy M Jeffries / Dmitri I Svergun / Gottfried Wilharm /
Abstract: Acinetobacter baumannii appears as an often multidrug-resistant nosocomial pathogen in hospitals worldwide. Its remarkable persistence in the hospital environment is probably due to intrinsic and ...Acinetobacter baumannii appears as an often multidrug-resistant nosocomial pathogen in hospitals worldwide. Its remarkable persistence in the hospital environment is probably due to intrinsic and acquired resistance to disinfectants and antibiotics, tolerance to desiccation stress, capability to form biofilms, and is possibly facilitated by surface-associated motility. Our attempts to elucidate surface-associated motility in A. baumannii revealed a mutant inactivated in a putative DNA-(adenine N6)-methyltransferase, designated A1S_0222 in strain ATCC 17978. We recombinantly produced A1S_0222 as a glutathione S-transferase (GST) fusion protein and purified it to near homogeneity through a combination of GST affinity chromatography, cation exchange chromatography and PD-10 desalting column. Furthermore we demonstrate A1S_0222-dependent adenine methylation at a GAATTC site. We propose the name AamA (Acinetobacteradenine methyltransferase A) in addition to the formal names M.AbaBGORF222P/M.Aba17978ORF8565P. Small angle X-ray scattering (SAXS) revealed that the protein is monomeric and has an extended and likely two-domain shape in solution.
Contact author
  • Cy M Jeffries (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
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Models

Model #1703
Type: dummy / Radius of dummy atoms: 2.75 A / Symmetry: P1 / Chi-square value: 1.062 / P-value: 0.132008
Search similar-shape structures of this assembly by Omokage search (details)
Model #1704
Type: dummy / Radius of dummy atoms: 2.75 A / Symmetry: P1 / Chi-square value: 1.062 / P-value: 0.132008
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: DNA-(adenine N6)-methyltransferase from Acinetobacter baumannii ATCC 17978
Specimen concentration: 2.4 mg/ml
BufferName: 150mM NaCl, 10mM Tris, 1mM DTT, 5% v/v glycerol / pH: 7.4
Entity #912Name: A1S_0222 / Type: protein / Description: DNA-(adenine N6)-methyltransferase / Formula weight: 48.902 / Num. of mol.: 1 / Source: Acinetobacter baumannii ATCC 17978
Sequence: MNSEPSVYHK RRHAARTTDE YLFHQLVPYL GNKRRLLHLI LEALEITGTL NSKKKNPPIF ADFFAGSGVV SRLARQNGYR VIANDWEPYS HALNHAILAC VDAPAFKELG GYQKAIDYLN RLPEVKGWVT HNLCPRNDDV YDPSRDRLFF KRRNGMRIDA IRQQIATWQA ...Sequence:
MNSEPSVYHK RRHAARTTDE YLFHQLVPYL GNKRRLLHLI LEALEITGTL NSKKKNPPIF ADFFAGSGVV SRLARQNGYR VIANDWEPYS HALNHAILAC VDAPAFKELG GYQKAIDYLN RLPEVKGWVT HNLCPRNDDV YDPSRDRLFF KRRNGMRIDA IRQQIATWQA QGAINDVEMS ALLAPLLYSA SFVSNTSGVF KSFHQGWGGR TQTALERIES LLWLTPSRFC EIGDRKRPAA EMWCVDAQHL ANQMSGFEVD VAYLDPPYNQ HAYSSNYHVL NALTLWDQVD LPPPDTKGYK SGIDRAWRKE RPSPYNSSKH AKDAYEKLLS TINARYILTS YSTDGNIEPK DLLMANLERG KVTLLTQDVP RYRVSKQRQS ERARVLEFIV ITDTHAKPGP PLRQLLGQLY HFAELGGVDT SGNSTQLALW

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3 mm
DetectorName: Pilatus 2M
Scan
Title: DNA-(adenine N6)-methyltransferase from Acinetobacter baumannii ATCC 17978
Measurement date: Sep 30, 2016 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0134 3.7925
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1471 /
MinMax
Q0.0739961 3.14662
P(R) point1 1471
R0 11.11
Result
Type of curve: single_conc
Comments: The individual DAMMIN models used to generate that averaged spatial representation of the protein (DAMFILT model) are included in the full entry zip archive as well as the refinement of the ...Comments: The individual DAMMIN models used to generate that averaged spatial representation of the protein (DAMFILT model) are included in the full entry zip archive as well as the refinement of the averaged structure using DAMSTART.
ExperimentalStandardPorod
MW52 kDa52 kDa-
Volume--96 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I03773 8 3765.76 6.6
Radius of gyration, Rg2.97 nm0.01 2.91 nm0.31

MinMax
D-11.11
Guinier point30 208

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