3kzc: Difference between revisions

<table><tr><td colspan='2'>[[3kzc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._ATCC_33913 Xanthomonas campestris pv. campestris str. ATCC 33913]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yh0 1yh0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZC FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>

<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=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=3kzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzc OCA], [https://pdbe.org/3kzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzc RCSB], [https://www.ebi.ac.uk/pdbsum/3kzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzc ProSAT]</span></td></tr>

[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.

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/3kzc_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kzc ConSurf].

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.

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<ref>PMID:15731101</ref>

==See Also==

*[[N-acetylornithine carbamoyltransferase|N-acetylornithine carbamoyltransferase]]

== References ==

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]]

[[Category: Allewell NM]]

[[Category: Shi D]]

[[Category: Tuchman M]]

[[Category: Yu X]]