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Structure paper

TitleThe Structure of NtdA, a Sugar Aminotransferase Involved in the Kanosamine Biosynthetic Pathway in Bacillus subtilis, Reveals a New Subclass of Aminotransferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 34121-34130, Year 2013
Publish dateApr 8, 2013 (structure data deposition date)
Authorsvan Straaten, K.E. / Ko, J.B. / Jagdhane, R. / Anjum, S. / Palmer, D.R. / Sanders, D.A.
External linksJ. Biol. Chem. / PubMed:24097983
MethodsX-ray diffraction
Resolution1.71 - 2.31 Å
Structure data

PDB-4k2b:
Crystal structure of ntda from bacillus subtilis in complex with the internal aldimine
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-4k2i:
Crystal structure of ntda from bacillus subtilis with bound cofactor pmp
Method: X-RAY DIFFRACTION / Resolution: 2.225 Å

PDB-4k2m:
Crystal structure of ntda from bacillus subtilis in complex with the plp external aldimine adduct with kanosamine-6-phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PMP:
4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE

ChemComp-ACT:
ACETATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-O1G:
3-deoxy-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-6-O-phosphono-alpha-D-gluco

Source
  • bacillus subtilis subsp. subtilis (bacteria)
KeywordsTRANSFERASE / Sugar aminotransferase / Aspertate aminotransferase fold / homo-dimer / additional N-terninal domain / 3-KETO-GLUCOSE-6-PHOSPHATE AMINITRANSFERASE / KANOSAMINE-6-PHOSPHATE

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