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1yh1

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{{Structure
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|RELATEDENTRY=[[1js1|1JS1]], [[1yh0|1YH0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yh1 OCA], [http://www.ebi.ac.uk/pdbsum/1yh1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yh1 RCSB]</span>
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'''Crystal Structure of Acetylornithine Transcarbamylase'''
'''Crystal Structure of Acetylornithine Transcarbamylase'''
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[[Category: Tuchman, M.]]
[[Category: Tuchman, M.]]
[[Category: Yu, X.]]
[[Category: Yu, X.]]
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[[Category: acetylcitrulline]]
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[[Category: Acetylcitrulline]]
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[[Category: acetylornithine]]
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[[Category: Acetylornithine]]
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[[Category: argf]]
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[[Category: Argf]]
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[[Category: transcarbamylase]]
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[[Category: Transcarbamylase]]
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Revision as of 13:18, 3 May 2008

Template:STRUCTURE 1yh1

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

1YH1 is a Single protein structure of sequence from Xanthomonas campestris. 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 Page seeded by OCA on Sat May 3 16:18:23 2008

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