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- SASDE92: Ribonuclease E from Acinetobacter baumannii (Endoribonuclease E, ... -

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Basic information

Entry
Database: SASBDB / ID: SASDE92
SampleRibonuclease E from Acinetobacter baumannii
  • Endoribonuclease E (protein), RNase E, Acinetobacter baumannii
Function / homology
Function and homology information


ribonuclease E / ribonuclease E activity / tRNA processing / mRNA catabolic process / RNA endonuclease activity / cytoplasmic side of plasma membrane / rRNA processing / tRNA binding / rRNA binding / magnesium ion binding ...ribonuclease E / ribonuclease E activity / tRNA processing / mRNA catabolic process / RNA endonuclease activity / cytoplasmic side of plasma membrane / rRNA processing / tRNA binding / rRNA binding / magnesium ion binding / zinc ion binding / cytoplasm
Similarity search - Function
Ribonuclease E/G / Ribonuclease E / RNA-binding protein AU-1/Ribonuclease E/G / Ribonuclease E/G family / RNA-binding domain, S1 / S1 domain profile. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / S1 domain / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
Biological speciesAcinetobacter baumannii (bacteria)
CitationDate: 2019 Dec
Title: A structural and biochemical comparison of Ribonuclease E homologues from pathogenic bacteria highlights species-specific properties
Authors: Mardle C / Shakespeare T / Butt L / Goddard L / Gowers D / Atkins H / Vincent H
Contact author
  • A Callaghan (University of Portsmouth)

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Structure visualization

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Models

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Sample

SampleName: Ribonuclease E from Acinetobacter baumannii / Specimen concentration: 5.52 mg/ml
BufferName: 10 mM DTT, 10 mM MgCl2, 0.5 M NaCl, 20 mM Tris / pH: 8
Entity #1207Name: RNase E / Type: protein / Description: Endoribonuclease E / Formula weight: 63.396 / Num. of mol.: 4 / Source: Acinetobacter baumannii / References: UniProt: A0A0B9WR03
Sequence: HHHHHHHHHH SSGHIEGRHM KRMLINATHA EEVRVALITG NRLYDFDLEN RTREQKKSNI YKGHVTRVEP SLEAVFVEYG AGRQGFLSMR EIANSYFQAD PRQTSNIREL ITEGTELLVQ VEKEERGNKG AALSTFISLA GRYLVLMPNN PKGGGISRQI SGSVREELKE ...Sequence:
HHHHHHHHHH SSGHIEGRHM KRMLINATHA EEVRVALITG NRLYDFDLEN RTREQKKSNI YKGHVTRVEP SLEAVFVEYG AGRQGFLSMR EIANSYFQAD PRQTSNIREL ITEGTELLVQ VEKEERGNKG AALSTFISLA GRYLVLMPNN PKGGGISRQI SGSVREELKE ILASLNVPRG MSVIVRTAGI GRTQEELQLD LQHLLDLWAQ IQGTASSGPS PMLVHQEAGV VTRAIRDYLR DDVAEILIDS EQAYNEAYNF VKAVMPRQLD KLKTYTLNEP LFAHFGIESQ IQTAYEREVK LPSGGSIVID QTEALVSIDI NSAKSTRGHD VEETALNTNL EAAEEIARQL RLRDIGGLVV IDFIDMTKER NQRMVEAKLR EATQSDRARI QFGQLSRFGL MEMSRQRLRP SLEEATGYVC PRCHGTGMVR DLRSLSLSIM RKVEEIALRE RHGEVQVEVP VEIAAFLLNE KRHSLVYLEQ TSGVRVTVLP HPHLETPHYE IAYNPDGFAP SSYERTEATR SSEKELGYES SEWHLEEADH GHAHVTATAS THAAAQKKAN HAT

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Experimental information

BeamInstrument name: Diamond Light Source B21 / City: Oxfordshire / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 4.014 mm
DetectorName: Pilatus 2M
Scan
Title: Ribonuclease E from Acinetobacter baumannii / Measurement date: Feb 11, 2017 / Storage temperature: 21 °C / Cell temperature: 15 °C / Exposure time: 3 sec. / Number of frames: 640 / Unit: 1/A /
MinMax
Q0.004 0.442
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 597 /
MinMax
Q0.00907336 0.15306
P(R) point1 597
R0 182.6
Result
Type of curve: single_conc /
ExperimentalPorod
MW298 kDa317 kDa
Volume-508 nm3

P(R)GuinierGuinier error
Forward scattering, I00.01877 0.0189 6.4E-5
Radius of gyration, Rg5.12 nm5.179 nm0.03

MinMax
D-18.26
Guinier point22 88

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