1yh0
From Proteopedia
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|PDB= 1yh0 |SIZE=350|CAPTION= <scene name='initialview01'>1yh0</scene>, resolution 2.20Å | |PDB= 1yh0 |SIZE=350|CAPTION= <scene name='initialview01'>1yh0</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1js1|1JS1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yh0 OCA], [http://www.ebi.ac.uk/pdbsum/1yh0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yh0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tuchman, M.]] | [[Category: Tuchman, M.]] | ||
[[Category: Yu, X.]] | [[Category: Yu, X.]] | ||
| - | [[Category: SO4]] | ||
[[Category: acetylcitrulline]] | [[Category: acetylcitrulline]] | ||
[[Category: acetylornithine]] | [[Category: acetylornithine]] | ||
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[[Category: transcarbamylase]] | [[Category: transcarbamylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:07:01 2008'' |
Revision as of 22:07, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Related: | 1JS1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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