Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Crystal structure of ErmE-23S rRNA methyltransferase in macrolide resistance
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Strukturbiologi. (Selmer)ORCID-id: 0000-0001-6560-011X
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Strukturbiologi.ORCID-id: 0000-0001-9079-2774
2019 (engelsk)Inngår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, nr 1, artikkel-id 14607Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Pathogens often receive antibiotic resistance genes through horizontal gene transfer from bacteria that produce natural antibiotics. ErmE is a methyltransferase (MTase) from Saccharopolyspora erythraea that dimethylates A2058 in 23S rRNA using S-adenosyl methionine (SAM) as methyl donor, protecting the ribosomes from macrolide binding. To gain insights into the mechanism of macrolide resistance, the crystal structure of ErmE was determined to 1.75 Å resolution. ErmE consists of an N-terminal Rossmann-like α/ß catalytic domain and a C-terminal helical domain. Comparison with ErmC' that despite only 24% sequence identity has the same function, reveals highly similar catalytic domains. Accordingly, superposition with the catalytic domain of ErmC' in complex with SAM suggests that the cofactor binding site is conserved. The two structures mainly differ in the C-terminal domain, which in ErmE contains a longer loop harboring an additional 310 helix that interacts with the catalytic domain to stabilize the tertiary structure. Notably, ErmE also differs from ErmC' by having long disordered extensions at its N- and C-termini. A C-terminal disordered region rich in arginine and glycine is also a present in two other MTases, PikR1 and PikR2, which share about 30% sequence identity with ErmE and methylate the same nucleotide in 23S rRNA.

sted, utgiver, år, opplag, sider
2019. Vol. 9, nr 1, artikkel-id 14607
HSV kategori
Forskningsprogram
Biologi med inriktning mot strukturbiologi
Identifikatorer
URN: urn:nbn:se:uu:diva-395134DOI: 10.1038/s41598-019-51174-0ISI: 000489555900001OAI: oai:DiVA.org:uu-395134DiVA, id: diva2:1360472
Forskningsfinansiär
Swedish Research Council, 2017-03827Swedish Research Council, 2016-06264Tilgjengelig fra: 2019-10-13 Laget: 2019-10-13 Sist oppdatert: 2019-11-08bibliografisk kontrollert

Open Access i DiVA

fulltext(4622 kB)46 nedlastinger
Filinformasjon
Fil FULLTEXT01.pdfFilstørrelse 4622 kBChecksum SHA-512
58b1d57ed9d7ea38e791ea6e55a5b98ffc7c9b7edc92fe355569c0251a6a98ce4b74ad63d9e257e50902641bec53cba3444978a793a6588f1e2b77290a0f2816
Type fulltextMimetype application/pdf
Supplementary material(1933 kB)2 nedlastinger
Filinformasjon
Fil ATTACHMENT01.pdfFilstørrelse 1933 kBChecksum SHA-512
a9df06e45c9d93049edcf4980a38738fc8bf8fd110e5bccd752d8b0271d95689e8c2b806bb84a976571cc232ef4c7f278cbdcb2b3b896abf501888d9e784cf4f
Type attachmentMimetype application/pdf

Andre lenker

Forlagets fulltekst

Søk i DiVA

Av forfatter/redaktør
Stsiapanava, AlenaSelmer, Maria
Av organisasjonen
I samme tidsskrift
Scientific Reports

Søk utenfor DiVA

GoogleGoogle Scholar
Totalt: 46 nedlastinger
Antall nedlastinger er summen av alle nedlastinger av alle fulltekster. Det kan for eksempel være tidligere versjoner som er ikke lenger tilgjengelige

doi
urn-nbn

Altmetric

doi
urn-nbn
Totalt: 64 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf