3m4j: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAO== | ==Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAO== | ||
<StructureSection load='3m4j' size='340' side='right' caption='[[3m4j]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3m4j' size='340' side='right'caption='[[3m4j]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3m4j]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3m4j]] 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=3M4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M4J FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m4j OCA], [https://pdbe.org/3m4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m4j RCSB], [https://www.ebi.ac.uk/pdbsum/3m4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m4j ProSAT]</span></td></tr> | |||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/3m4j_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/3m4j_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 32: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 3m4j" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3m4j" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[N-acetylornithine carbamoyltransferase|N-acetylornithine carbamoyltransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Xanthomonas campestris pv. campestris]] | ||
[[Category: Allewell | [[Category: Allewell NM]] | ||
[[Category: Li | [[Category: Li Y]] | ||
[[Category: Shi | [[Category: Shi D]] | ||
[[Category: Tuchman | [[Category: Tuchman M]] | ||
[[Category: Yu | [[Category: Yu X]] | ||
Latest revision as of 11:48, 6 September 2023
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAOCrystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAO
Structural highlights
FunctionAOTC_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 PubMedN-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 AlsoReferences
|
| ||||||||||||||||||