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Structure paper

TitleHeme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival.
Journal, issue, pagesCommun Biol, Vol. 4, Page 467-467, Year 2021
Publish dateJan 15, 2021 (structure data deposition date)
AuthorsNishinaga, M. / Sugimoto, H. / Nishitani, Y. / Nagai, S. / Nagatoishi, S. / Muraki, N. / Tosha, T. / Tsumoto, K. / Aono, S. / Shiro, Y. / Sawai, H.
External linksCommun Biol / PubMed:33850260
MethodsX-ray diffraction
Resolution1.7 - 2.6 Å
Structure data

PDB-7dvr:
Crystal structure of heme sensor protein PefR from Streptococcus agalactiae in complex with heme
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-7dvs:
Crystal structure of Apo (heme-free) PefR
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7dvt:
Crystal structure of heme sensor protein PefR in complex with heme and carbon monoxide
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-7dvu:
Crystal structure of heme sensor protein PefR in complex with heme and cyanide
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-7dvv:
Heme sensor protein PefR from Streptococcus agalactiae bound to operator DNA (28-mer)
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CO:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CMO:
CARBON MONOXIDE

ChemComp-CYN:
CYANIDE ION

Source
  • streptococcus agalactiae serotype iii (strain nem316) (bacteria)
  • streptococcus agalactiae (bacteria)
  • streptococcus agalactiae nem316 (bacteria)
KeywordsTRANSCRIPTION / heme-binding / helix-turn-helix / Heme / transcription regulator

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