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- SASDE52: Ribonuclease E from Escherichia coli (Endoribonuclease E, RNase E) -

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Open data


ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDE52
SampleRibonuclease E from Escherichia coli
  • Endoribonuclease E (protein), RNase E, Escherichia coli
Function / homology
Function and homology information


regulation of RNA helicase activity / rRNA 5'-end processing / bacterial degradosome / ribonuclease E / ribonuclease E activity / endoribonuclease complex / DEAD/H-box RNA helicase binding / 7S RNA binding / RNA catabolic process / tRNA processing ...regulation of RNA helicase activity / rRNA 5'-end processing / bacterial degradosome / ribonuclease E / ribonuclease E activity / endoribonuclease complex / DEAD/H-box RNA helicase binding / 7S RNA binding / RNA catabolic process / tRNA processing / mRNA catabolic process / protein complex oligomerization / RNA nuclease activity / RNA processing / RNA endonuclease activity / cytoplasmic side of plasma membrane / rRNA processing / protein homotetramerization / molecular adaptor activity / tRNA binding / rRNA binding / magnesium ion binding / RNA binding / zinc ion binding / identical protein binding / membrane / cytoplasm
Similarity search - Function
Polyribonucleotide phosphorylase C-terminal / Polyribonucleotide phosphorylase C terminal / : / RNase E/G, Thioredoxin-like domain / Ribonuclease E/G / Ribonuclease E / RNA-binding protein AU-1/Ribonuclease E/G / Ribonuclease E/G family / S1 domain profile. / Ribosomal protein S1-like RNA-binding domain ...Polyribonucleotide phosphorylase C-terminal / Polyribonucleotide phosphorylase C terminal / : / RNase E/G, Thioredoxin-like domain / Ribonuclease E/G / Ribonuclease E / RNA-binding protein AU-1/Ribonuclease E/G / Ribonuclease E/G family / 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 speciesEscherichia coli (E. coli)
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

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #2185
Type: dummy / Software: (5) / Radius of dummy atoms: 5.00 A / Symmetry: P222 / Chi-square value: 1.054 / P-value: 0.000144
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Ribonuclease E from Escherichia coli / Specimen concentration: 6.58 mg/ml
BufferName: 10 mM DTT, 10 mM MgCl2, 0.5 M NaCl, 20 mM Tris / pH: 8
Entity #1203Name: RNase E / Type: protein / Description: Endoribonuclease E / Formula weight: 61.84 / Num. of mol.: 4 / Source: Escherichia coli / References: UniProt: P21513
Sequence: HHHHHHHHHH SSGHIEGRHM KRMLINATQQ EELRVALVDG QRLYDLDIES PGHEQKKANI YKGKITRIEP SLEAAFVDYG AERHGFLPLK EIAREYFPAN YSAHGRPNIK DVLREGQEVI VQIDKEERGN KGAALTTFIS LAGSYLVLMP NNPRAGGISR RIEGDDRTEL ...Sequence:
HHHHHHHHHH SSGHIEGRHM KRMLINATQQ EELRVALVDG QRLYDLDIES PGHEQKKANI YKGKITRIEP SLEAAFVDYG AERHGFLPLK EIAREYFPAN YSAHGRPNIK DVLREGQEVI VQIDKEERGN KGAALTTFIS LAGSYLVLMP NNPRAGGISR RIEGDDRTEL KEALASLELP EGMGLIVRTA GVGKSAEALQ WDLSFRLKHW EAIKKAAESR PAPFLIHQES NVIVRAFRDY LRQDIGEILI DNPKVLELAR QHIAALGRPD FSSKIKLYTG EIPLFSHYQI ESQIESAFQR EVRLPSGGSI VIDSTEALTA IDINSARATR GGDIEETAFN TNLEAADEIA RQLRLRDLGG LIVIDFIDMT PVRHQRAVEN RLREAVRQDR ARIQISHISR FGLLEMSRQR LSPSLGESSH HVCPRCSGTG TVRDNESLSL SILRLIEEEA LKENTQEVHA IVPVPIASYL LNEKRSAVNA IETRQDGVRC VIVPNDQMET PHYHVLRVRK GEETPTLSYM LPKLHEEAMA LPSEEEFAER KRPEQPAL

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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 Escherichia coli / 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 4.6 / Number of points: 454 /
MinMax
Q0.004362 0.4419
P(R) point1 454
R0 161
Result
Type of curve: single_conc /
ExperimentalPorod
MW276 kDa290 kDa
Volume-468 nm3

P(R)GuinierGuinier error
Forward scattering, I00.04441 0.04445 6.8E-5
Radius of gyration, Rg5.01 nm5.031 nm0.215

MinMax
D-16.1
Guinier point16 91

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