1yh0
From Proteopedia
(New page: 200px<br /><applet load="1yh0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yh0, resolution 2.20Å" /> '''Crystal Structure of...) |
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| - | [[Image:1yh0.gif|left|200px]]<br /><applet load="1yh0" size=" | + | [[Image:1yh0.gif|left|200px]]<br /><applet load="1yh0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yh0, resolution 2.20Å" /> | caption="1yh0, resolution 2.20Å" /> | ||
'''Crystal Structure of Acetylornithine Transcarbamylase'''<br /> | '''Crystal Structure of Acetylornithine Transcarbamylase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have identified in Xanthomonas campestris a novel N-acetylornithine | + | 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== | ==About this Structure== | ||
| - | 1YH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YH0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YH0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthomonas campestris]] | [[Category: Xanthomonas campestris]] | ||
| - | [[Category: Allewell, N | + | [[Category: Allewell, N M.]] |
[[Category: Caldovic, L.]] | [[Category: Caldovic, L.]] | ||
| - | [[Category: Malamy, M | + | [[Category: Malamy, M H.]] |
[[Category: Morizono, H.]] | [[Category: Morizono, H.]] | ||
[[Category: Roth, L.]] | [[Category: Roth, L.]] | ||
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[[Category: transcarbamylase]] | [[Category: transcarbamylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:13 2008'' |
Revision as of 14:05, 21 February 2008
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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 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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