|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2w37' size='340' side='right'caption='[[2w37]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2w37' size='340' side='right'caption='[[2w37]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w37]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"lactobacillus_type_ii"_fornachon_1943 "lactobacillus type ii" fornachon 1943]. 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> | + | <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='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> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] </span></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> | | <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> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lactobacillus type ii fornachon 1943]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ornithine carbamoyltransferase]] | + | [[Category: Lentilactobacillus hilgardii]] |
| - | [[Category: Angulo, I]] | + | [[Category: Angulo I]] |
| - | [[Category: Fox, G C]] | + | [[Category: Fox GC]] |
| - | [[Category: Mancheno, J M]] | + | [[Category: Mancheno JM]] |
| - | [[Category: Munoz, R]] | + | [[Category: Munoz R]] |
| - | [[Category: Rivas, B de las]]
| + | [[Category: Rodriguez H]] |
| - | [[Category: Rodriguez, H]] | + | [[Category: De las Rivas B]] |
| - | [[Category: Arginine metabolism]] | + | |
| - | [[Category: Carbamoyl phosphate]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Metal binding-site]]
| + | |
| - | [[Category: Ornithine]]
| + | |
| - | [[Category: Transcarbamylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1]
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
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ de Las Rivas B, Fox GC, Angulo I, Ripoll MM, Rodriguez H, Munoz R, Mancheno JM. Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding. J Mol Biol. 2009 Oct 23;393(2):425-34. Epub 2009 Aug 8. PMID:19666033 doi:10.1016/j.jmb.2009.08.002
- ↑ de Las Rivas B, Fox GC, Angulo I, Ripoll MM, Rodriguez H, Munoz R, Mancheno JM. Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding. J Mol Biol. 2009 Oct 23;393(2):425-34. Epub 2009 Aug 8. PMID:19666033 doi:10.1016/j.jmb.2009.08.002
|
