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TitleStructures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.
Journal, issue, pagesProteins, Vol. 64, Page 532-542, Year 2006
Publish dateDec 8, 2009 (structure data deposition date)
AuthorsShi, D. / Yu, X. / Roth, L. / Morizono, H. / Tuchman, M. / Allewell, N.M.
External linksProteins / PubMed:16741992
MethodsX-ray diffraction
Resolution1.8 - 1.95 Å
Structure data

PDB-3kzm:
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3kzn:
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with N-acetyl-L-ornirthine
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3kzo:
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CP:
PHOSPHORIC ACID MONO(FORMAMIDE)ESTER

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-AOR:
N~2~-ACETYL-L-ORNITHINE

ChemComp-AN0:
N-ACETYL-L-NORVALINE

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

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