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| - | [[Image:1yh1.gif|left|200px]] | + | #REDIRECT [[3kzk]] This PDB entry is obsolete and replaced by 3kzk |
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| - | {{Structure
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| - | |PDB= 1yh1 |SIZE=350|CAPTION= <scene name='initialview01'>1yh1</scene>, resolution 1.90Å
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| - | |SITE=
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| - | |LIGAND= <scene name='pdbligand=OLN:(S)-2-ACETAMIDO-5-UREIDOPENTANOIC+ACID'>OLN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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| - | |ACTIVITY=
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| - | |GENE=
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| - | |DOMAIN=
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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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| - | }}
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| - | '''Crystal Structure of Acetylornithine Transcarbamylase'''
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| - | ==Overview==
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| - | 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.
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| - | ==About this Structure==
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| - | 1YH1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YH1 OCA].
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| - | ==Reference==
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| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15731101 15731101]
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| - | [[Category: Single protein]]
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| - | [[Category: Xanthomonas campestris]]
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| - | [[Category: Allewell, N M.]]
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| - | [[Category: Caldovic, L.]]
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| - | [[Category: Malamy, M H.]]
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| - | [[Category: Morizono, H.]]
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| - | [[Category: Roth, L.]]
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| - | [[Category: Shi, D.]]
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| - | [[Category: Tuchman, M.]]
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| - | [[Category: Yu, X.]]
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| - | [[Category: acetylcitrulline]]
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| - | [[Category: acetylornithine]]
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| - | [[Category: argf]]
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| - | [[Category: transcarbamylase]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:07:02 2008''
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