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| | <StructureSection load='3m4n' size='340' side='right'caption='[[3m4n]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3m4n' size='340' side='right'caption='[[3m4n]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M4N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3m4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M4N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m4j|3m4j]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m4n OCA], [https://pdbe.org/3m4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m4n RCSB], [https://www.ebi.ac.uk/pdbsum/3m4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m4n ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m4n OCA], [https://pdbe.org/3m4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m4n RCSB], [https://www.ebi.ac.uk/pdbsum/3m4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m4n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP]] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
| + | [https://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylornithine carbamoyltransferase]] | + | [[Category: Xanthomonas campestris pv. campestris]] |
| - | [[Category: Xance]]
| + | [[Category: Allewell NM]] |
| - | [[Category: Allewell, N M]] | + | [[Category: Li Y]] |
| - | [[Category: Li, Y]] | + | [[Category: Shi D]] |
| - | [[Category: Shi, D]] | + | [[Category: Tuchman M]] |
| - | [[Category: Tuchman, M]] | + | [[Category: Yu X]] |
| - | [[Category: Yu, X]] | + | |
| - | [[Category: Amino-acid biosynthesis]]
| + | |
| - | [[Category: Arginine biosynthesis]]
| + | |
| - | [[Category: Transcarbamylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AOTC_XANCP Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
N-Acetyl-l-ornithine transcarbamylase (AOTCase), rather than ornithine transcarbamylase (OTCase), is the essential carbamylase enzyme in the arginine biosynthesis of several plant and human pathogens. The specificity of this unique enzyme provides a potential target for controlling the spread of these pathogens. Recently, several crystal structures of AOTCase from Xanthomonas campestris (xc) have been determined. In these structures, an unexplained electron density at the tip of the Lys302 side chain was observed. Using (13)C NMR spectroscopy, we show herein that Lys302 is post-translationally carboxylated. The structure of wild-type AOTCase in a complex with the bisubstrate analogue N(delta)-(phosphonoacetyl)-N(alpha)-acetyl-l-ornithine (PALAO) indicates that the carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. Furthermore, the carboxyl group is involved in binding N-acetyl-l-ornithine via a water molecule. Activity assays with the wild-type enzyme and several mutants demonstrate that the post-translational modification of lysine 302 has an important role in catalysis.
Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.,Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D Biochemistry. 2010 Aug 17;49(32):6887-95. PMID:20695527[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D. Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry. 2010 Aug 17;49(32):6887-95. PMID:20695527 doi:10.1021/bi1007386
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