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| | <StructureSection load='3vpc' size='340' side='right'caption='[[3vpc]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='3vpc' size='340' side='right'caption='[[3vpc]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vpc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_16993 Dsm 16993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vpc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii Sulfurisphaera tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 1.87Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vpb|3vpb]], [[3vpd|3vpd]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ArgX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=111955 DSM 16993])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylornithine_deacetylase Acetylornithine deacetylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.16 3.5.1.16] </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=3vpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpc OCA], [https://pdbe.org/3vpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpc RCSB], [https://www.ebi.ac.uk/pdbsum/3vpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpc 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=3vpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpc OCA], [https://pdbe.org/3vpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpc RCSB], [https://www.ebi.ac.uk/pdbsum/3vpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ARGX_SULTO ARGX_SULTO]] Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW (By similarity).
| + | [https://www.uniprot.org/uniprot/ARGX_SULTO ARGX_SULTO] Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetylornithine deacetylase]] | |
| - | [[Category: Dsm 16993]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Horie, A]] | + | [[Category: Sulfurisphaera tokodaii]] |
| - | [[Category: Kuzuyama, T]] | + | [[Category: Horie A]] |
| - | [[Category: Nishiyama, M]] | + | [[Category: Kuzuyama T]] |
| - | [[Category: Tomita, T]] | + | [[Category: Nishiyama M]] |
| - | [[Category: Atp-dependenet amine/thiol ligase]]
| + | [[Category: Tomita T]] |
| - | [[Category: Atp-dependenet amine/thiol ligase family]]
| + | |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
ARGX_SULTO Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW (By similarity).
Publication Abstract from PubMed
LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of alpha-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX.
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.,Ouchi T, Tomita T, Horie A, Yoshida A, Takahashi K, Nishida H, Lassak K, Taka H, Mineki R, Fujimura T, Kosono S, Nishiyama C, Masui R, Kuramitsu S, Albers SV, Kuzuyama T, Nishiyama M Nat Chem Biol. 2013 Apr;9(4):277-83. doi: 10.1038/nchembio.1200. Epub 2013 Feb, 24. PMID:23434852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ouchi T, Tomita T, Horie A, Yoshida A, Takahashi K, Nishida H, Lassak K, Taka H, Mineki R, Fujimura T, Kosono S, Nishiyama C, Masui R, Kuramitsu S, Albers SV, Kuzuyama T, Nishiyama M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat Chem Biol. 2013 Apr;9(4):277-83. doi: 10.1038/nchembio.1200. Epub 2013 Feb, 24. PMID:23434852 doi:10.1038/nchembio.1200
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