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| | ==Structure of the ornithine carbamoyltransferase from Mycoplasma penetrans with a P23 Space group== | | ==Structure of the ornithine carbamoyltransferase from Mycoplasma penetrans with a P23 Space group== |
| - | <StructureSection load='4anf' size='340' side='right' caption='[[4anf]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4anf' size='340' side='right'caption='[[4anf]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4anf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycoplasma_penetrans Mycoplasma penetrans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ANF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4anf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Malacoplasma_penetrans Malacoplasma penetrans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ANF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ANF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4amu|4amu]]</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]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] </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=4anf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4anf OCA], [https://pdbe.org/4anf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4anf RCSB], [https://www.ebi.ac.uk/pdbsum/4anf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4anf ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4anf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4anf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4anf RCSB], [http://www.ebi.ac.uk/pdbsum/4anf PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OTCC_MYCPE OTCC_MYCPE]] Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | + | [https://www.uniprot.org/uniprot/OTCC_MALP2 OTCC_MALP2] nvolved 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:23082227</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4anf" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ornithine carbamoyltransferase|Ornithine carbamoyltransferase]] | + | *[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycoplasma penetrans]] | + | [[Category: Large Structures]] |
| - | [[Category: Ornithine carbamoyltransferase]] | + | [[Category: Malacoplasma penetrans]] |
| - | [[Category: Benach, J]] | + | [[Category: Benach J]] |
| - | [[Category: Gallego, P]] | + | [[Category: Gallego P]] |
| - | [[Category: Perez-Pons, J A]] | + | [[Category: Perez-Pons JA]] |
| - | [[Category: Planell, R]] | + | [[Category: Planell R]] |
| - | [[Category: Querol, E]] | + | [[Category: Querol E]] |
| - | [[Category: Reverter, D]] | + | [[Category: Reverter D]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ornithine transcarbamylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
OTCC_MALP2 nvolved 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]
Publication Abstract from PubMed
The metabolism of arginine towards ATP synthesis has been considered a major source of energy for microorganisms such as Mycoplasma penetrans in anaerobic conditions. Additionally, this pathway has also been implicated in pathogenic and virulence mechanism of certain microorganisms, i.e. protection from acidic stress during infection. In this work we present the crystal structures of the three enzymes composing the gene cluster of the arginine deiminase pathway from M. penetrans: arginine deiminase (ADI), ornithine carbamoyltransferase (OTC) and carbamate kinase (CK). The arginine deiminase (ADI) structure has been refined to 2.3 A resolution in its apo-form, displaying an "open" conformation of the active site of the enzyme in comparison to previous complex structures with substrate intermediates. The active site pocket of ADI is empty, with some of the catalytic and binding residues far from their active positions, suggesting major conformational changes upon substrate binding. Ornithine carbamoyltransferase (OTC) has been refined in two crystal forms at 2.5 A and 2.6 A resolution, respectively, both displaying an identical dodecameric structure with a 23-point symmetry. The dodecameric structure of OTC represents the highest level of organization in this protein family and in M.penetrans it is constituted by a novel interface between the four catalytic homotrimers. Carbamate kinase (CK) has been refined to 2.5 A resolution and its structure is characterized by the presence of two ion sulfates in the active site, one in the carbamoyl phosphate binding site and the other in the beta-phosphate ADP binding pocket of the enzyme. The CK structure also shows variations in some of the elements that regulate the catalytic activity of the enzyme. The relatively low number of metabolic pathways and the relevance in human pathogenesis of Mycoplasma penetrans places the arginine deiminase pathway enzymes as potential targets to design specific inhibitors against this human parasite.
Structural Characterization of the Enzymes Composing the Arginine Deiminase Pathway in Mycoplasma penetrans.,Gallego P, Planell R, Benach J, Querol E, Perez-Pons JA, Reverter D PLoS One. 2012;7(10):e47886. doi: 10.1371/journal.pone.0047886. Epub 2012 Oct 17. PMID:23082227[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gallego P, Planell R, Benach J, Querol E, Perez-Pons JA, Reverter D. Structural Characterization of the Enzymes Composing the Arginine Deiminase Pathway in Mycoplasma penetrans. PLoS One. 2012;7(10):e47886. doi: 10.1371/journal.pone.0047886. Epub 2012 Oct 17. PMID:23082227 doi:http://dx.doi.org/10.1371/journal.pone.0047886
- ↑ Gallego P, Planell R, Benach J, Querol E, Perez-Pons JA, Reverter D. Structural Characterization of the Enzymes Composing the Arginine Deiminase Pathway in Mycoplasma penetrans. PLoS One. 2012;7(10):e47886. doi: 10.1371/journal.pone.0047886. Epub 2012 Oct 17. PMID:23082227 doi:http://dx.doi.org/10.1371/journal.pone.0047886
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