PMID:15731101
| Citation |
Shi, D, Morizono, H, Yu, X, Roth, L, Caldovic, L, Allewell, NM, Malamy, MH and Tuchman, M (2005) Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. J. Biol. Chem. 280:14366-9 |
|---|---|
| Abstract |
We have identified in Xanthomonas campestris a novel N-acetylornithine transcarbamylase that replaces ornithine transcarbamylase in the canonic arginine biosynthetic pathway of several Eubacteria. The crystal structures of the protein in the presence and absence of the reaction product, N-acetylcitrulline, were determined. This new family of transcarbamylases lacks the DxxSMG motif that is characteristic of all ornithine transcarbamylases (OTCases) and contains a novel proline-rich loop that forms part of the active site. The specificity for N-acetylornithine is conferred by hydrogen bonding with residues in the proline-rich loop via water molecules and by hydrophobic interactions with residues from the adjacent 80's, 120's, and proline-rich loops. This novel protein structure provides a starting point for rational design of specific analogs that may be useful in combating human and plant pathogens that utilize acetylornithine transcarbamylase rather than ornithine transcarbamylase. |
| Links |
PubMed Online version:10.1074/jbc.C500005200 |
| Keywords |
Binding Sites; Carboxyl and Carbamoyl Transferases/chemistry; Cloning, Molecular; Crystallography, X-Ray; Ligands; Models, Molecular; Ornithine Carbamoyltransferase/chemistry; Proline/chemistry; Protein Conformation; Protein Structure, Secondary; Water/chemistry; Xanthomonas campestris/enzymology |
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