2w37
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2w37 is ON HOLD until Paper Publication Authors: delasRivas, B., Fox, G.C., Angulo, I., Rodriguez, H., Munoz, R., Mancheno, J.M. Description: CRYST...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE TRANSCARBAMYLASE FROM Lactobacillus hilgardii== | |
| + | <StructureSection load='2w37' size='340' side='right'caption='[[2w37]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2w37]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentilactobacillus_hilgardii Lentilactobacillus hilgardii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W37 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=2w37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w37 OCA], [https://pdbe.org/2w37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w37 RCSB], [https://www.ebi.ac.uk/pdbsum/2w37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w37 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OTCC_LENHI OTCC_LENHI] Involved in the catabolism of arginine. Catalyzes the phosphorolysis of citrulline, the reverse reaction of the biosynthetic one, yielding ornithine and carbamoyl phosphate which serve to generate ATP from ADP.<ref>PMID:19666033</ref> | ||
| + | == 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/w3/2w37_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=2w37 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catabolic ornithine transcarbamylase (cOTC; EC 2.1.3.3) catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii (Lh-cOTC) refined to 2.1 A resolution. The structure reveals that Lh-cOTC forms a hexameric assembly, which was also confirmed by gel-filtration chromatography and analytical ultracentrifugation. The homohexamer, with 32 point group symmetry, represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution. Additionally, the structure reveals, for the first time in the ornithine transcarbamylase family, a metal-binding site located at the 3-fold molecular symmetry axis of each trimer. | ||
| - | + | Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding.,de Las Rivas B, Fox GC, Angulo I, Ripoll MM, Rodriguez H, Munoz R, Mancheno JM J Mol Biol. 2009 Oct 23;393(2):425-34. Epub 2009 Aug 8. PMID:19666033<ref>PMID:19666033</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2w37" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lentilactobacillus hilgardii]] | ||
| + | [[Category: Angulo I]] | ||
| + | [[Category: Fox GC]] | ||
| + | [[Category: Mancheno JM]] | ||
| + | [[Category: Munoz R]] | ||
| + | [[Category: Rodriguez H]] | ||
| + | [[Category: De las Rivas B]] | ||
Current revision
CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE TRANSCARBAMYLASE FROM Lactobacillus hilgardii
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