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| | <StructureSection load='3vpb' size='340' side='right'caption='[[3vpb]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3vpb' size='340' side='right'caption='[[3vpb]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPB 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>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vpc|3vpc]], [[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>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argE, STK_15050 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO]), lysW, STK_01925, STS023 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [https://pdbe.org/3vpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [https://www.ebi.ac.uk/pdbsum/3vpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpb 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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [https://pdbe.org/3vpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [https://www.ebi.ac.uk/pdbsum/3vpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpb 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/LYSW_SULTO LYSW_SULTO]] Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-arginine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
| + | [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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulto]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Kuzuyama, T]] | + | [[Category: Kuzuyama T]] |
| - | [[Category: Nishiyama, M]] | + | [[Category: Nishiyama M]] |
| - | [[Category: Ouchi, T]] | + | [[Category: Ouchi T]] |
| - | [[Category: Tomita, T]] | + | [[Category: Tomita T]] |
| - | [[Category: Atp-dependent amine/thiol ligase]]
| + | |
| - | [[Category: Atp-dependent amine/thiol ligase family]]
| + | |
| - | [[Category: Enzyme-carrier protein complex]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Lysw]]
| + | |
| Structural highlights
3vpb is a 6 chain structure with sequence from Sulfurisphaera tokodaii str. 7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.8Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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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