1yh0

From Proteopedia

Revision as of 04:38, 21 November 2007

Crystal Structure of Acetylornithine Transcarbamylase

Overview

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.

About this Structure

1YH0 is a Single protein structure of sequence from Xanthomonas campestris with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria., Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH, Tuchman M, J Biol Chem. 2005 Apr 15;280(15):14366-9. Epub 2005 Feb 24. PMID:15731101

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