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Structure paper

TitleCrystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria.
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 14366-14369, Year 2005
Publish dateDec 8, 2009 (structure data deposition date)
AuthorsShi, D. / Morizono, H. / Yu, X. / Roth, L. / Caldovic, L. / Allewell, N.M. / Malamy, M.H. / Tuchman, M.
External linksJ. Biol. Chem. / PubMed:15731101
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-3kzc:
Crystal structure of N-acetyl-L-ornithine transcarbamylase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3kzk:
Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-OLN:
(S)-2-ACETAMIDO-5-UREIDOPENTANOIC ACID

Source
  • xanthomonas campestris pv. campestris (bacteria)
KeywordsTRANSFERASE / transcarbamylase / Amino-acid biosynthesis / Arginine biosynthesis / Cytoplasm

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