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TitleaKMT Catalyzes Extensive Protein Lysine Methylation in the Hyperthermophilic Archaeon Sulfolobus islandicus but is Dispensable for the Growth of the Organism
Journal, issue, pagesMol. Cell Proteomics, Vol. 15, Page 2908-2923, Year 2016
Publish dateDec 11, 2015 (structure data deposition date)
AuthorsChu, Y. / Zhu, Y. / Chen, Y. / Li, W. / Zhang, Z. / Liu, D. / Wang, T. / Ma, J. / Deng, H. / Liu, Z.J. ...Chu, Y. / Zhu, Y. / Chen, Y. / Li, W. / Zhang, Z. / Liu, D. / Wang, T. / Ma, J. / Deng, H. / Liu, Z.J. / Ouyang, S. / Huang, L.
External linksMol. Cell Proteomics / PubMed:27329856
MethodsX-ray diffraction
Resolution1.3 - 1.87 Å
Structure data

PDB-5fa8:
SAM complex with aKMT from the hyperthermophilic archaeon Sulfolobus islandicu
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-5fad:
SAH complex with aKMT from the hyperthermophilic archaeon Sulfolobus islandicus
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • sulfolobus islandicus (strain m.14.25 / kamchatka #1) (acidophilic)
KeywordsTRANSFERASE / protein methyltransferase

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