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TitleHow Oligomerization Contributes to the Thermostability of an Archaeon Protein: PROTEIN L-ISOASPARTYL-O-METHYLTRANSFERASE FROM SULFOLOBUS TOKODAII
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 32957-32967, Year 2004
Publish dateFeb 25, 2004 (structure data deposition date)
AuthorsTanaka, Y. / Tsumoto, K. / Yasutake, Y. / Umetsu, M. / Yao, M. / Fukada, H. / Tanaka, I. / Kumagai, I.
External linksJ. Biol. Chem. / PubMed:15169774
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1vbf:
Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • sulfolobus tokodaii (archaea)
KeywordsTRANSFERASE / trimeric coiled coil assembly / inter-subunit disulfide bridge / protein repair enzyme

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