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TitleStructure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.
Journal, issue, pagesFebs Lett., Vol. 582, Page 623-626, Year 2008
Publish dateJan 15, 2008 (structure data deposition date)
AuthorsNguyen, L. / Kozlov, G. / Gehring, K.
External linksFebs Lett. / PubMed:18242192
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-3bxy:
Crystal structure of tetrahydrodipicolinate N-succinyltransferase from E. coli
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / left-handed beta-helix / Structural Genomics / CIHR / Canadian Institutes of Health Research / Montreal-Kingston Bacterial Structural Genomics Initiative / BSGI / Acyltransferase / Amino-acid biosynthesis / Diaminopimelate biosynthesis / Lysine biosynthesis

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