Summary for 3KZC
| Entry DOI | 10.2210/pdb3kzc/pdb |
| Related | 2FG7 3KZK 3KZM 3KZN 3KZO 3L02 3L04 3L05 3L06 |
| Descriptor | N-acetylornithine carbamoyltransferase, SULFATE ION (3 entities in total) |
| Functional Keywords | transcarbamylase, amino-acid biosynthesis, arginine biosynthesis, cytoplasm, transferase |
| Biological source | Xanthomonas campestris pv. campestris |
| Cellular location | Cytoplasm : Q8P8J2 |
| Total number of polymer chains | 1 |
| Total formula weight | 40325.70 |
| Authors | Shi, D.,Yu, X.,Allewell, N.M.,Tuchman, M. (deposition date: 2009-12-08, release date: 2010-03-31, Last modification date: 2023-11-22) |
| Primary citation | Shi, D.,Morizono, H.,Yu, X.,Roth, L.,Caldovic, L.,Allewell, N.M.,Malamy, M.H.,Tuchman, M. 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., 280:14366-14369, 2005 Cited by PubMed 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. PubMed: 15731101DOI: 10.1074/jbc.C500005200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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