3kzo
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3kzo is ON HOLD Authors: Shi, D., Yu, X., Allewell, N.M., Tuchman, M. Description: Crystal structure of N-acetyl-L-ornithine transcarbamylase compl...) |
|||
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline== | |
| + | <StructureSection load='3kzo' size='340' side='right'caption='[[3kzo]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3kzo]] 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=1zq8 1zq8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZO 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]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AN0:N-ACETYL-L-NORVALINE'>AN0</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=3kzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzo OCA], [https://pdbe.org/3kzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzo RCSB], [https://www.ebi.ac.uk/pdbsum/3kzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/3kzo_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3kzo ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the transcarbamoylase superfamily that is essential for arginine biosynthesis in several eubacteria. We report here crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or N-acetyl-L-ornithine (AORN), and the ternary complex with CP and N-acetyl-L-norvaline. Comparison of these structures demonstrates that the substrate-binding mechanism of this novel transcarbamoylase is different from those of aspartate and ornithine transcarbamoylases, both of which show ordered substrate binding with large domain movements. CP and AORN bind to AOTCase independently, and the main conformational change upon substrate binding is ordering of the 80's loop, with a small domain closure around the active site and little movement of the 240's loop. The structures of the complexes provide insight into the mode of substrate binding and the mechanism of the transcarbamoylation reaction. | ||
| - | + | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.,Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM Proteins. 2006 Aug 1;64(2):532-42. PMID:16741992<ref>PMID:16741992</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3kzo" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[N-acetylornithine carbamoyltransferase|N-acetylornithine carbamoyltransferase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]] | ||
| + | [[Category: Allewell NM]] | ||
| + | [[Category: Shi D]] | ||
| + | [[Category: Tuchman M]] | ||
| + | [[Category: Yu X]] | ||
Current revision
Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline
| |||||||||||
