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Structure paper

TitleStructures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 64, Page 397-406, Year 2008
Publish dateMay 13, 2004 (structure data deposition date)
AuthorsKishishita, S. / Shimizu, K. / Murayama, K. / Terada, T. / Shirouzu, M. / Yokoyama, S. / Kunishima, N.
External linksActa Crystallogr. ,Sect. D / PubMed:18391406
MethodsX-ray diffraction
Resolution2 - 2.1 Å
Structure data

PDB-1wde:
Crystal structure of the conserved hypothetical protein APE0931 from Aeropyrum pernix K1
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1wng:
Structural study of project ID PH0725 from Pyrococcus horikoshii OT3
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • aeropyrum pernix (archaea)
  • pyrococcus horikoshii (archaea)
KeywordsTRANSFERASE / Structural genomics / conserved hypothetical protein / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Methyltransferase / NPPSFA / National Project on Protein Structural and Functional Analyses

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