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| | <StructureSection load='1tz3' size='340' side='right'caption='[[1tz3]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1tz3' size='340' side='right'caption='[[1tz3]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tz3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TZ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tz3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TZ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIS:5-AMINOIMIDAZOLE+RIBONUCLEOSIDE'>AIS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIS:5-AMINOIMIDAZOLE+RIBONUCLEOSIDE'>AIS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tyy|1tyy]], [[1tz6|1tz6]]</div></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=1tz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tz3 OCA], [https://pdbe.org/1tz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tz3 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stm4066 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructokinase Fructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.4 2.7.1.4] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tz3 OCA], [http://pdbe.org/1tz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tz3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AIRSK_SALTY AIRSK_SALTY] Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the purine and thiamine biosynthetic pathways (PubMed:12486071). It allows the use of exogenous aminoimidazole riboside (AIRs) to satisfy the cellular requirement for purines and thiamine (PubMed:12486071).<ref>PMID:12486071</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fructokinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Dougherty, M]] | + | [[Category: Dougherty M]] |
| - | [[Category: Downs, D M]] | + | [[Category: Downs DM]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Ealick SE]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Ribokinase fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AIRSK_SALTY Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the purine and thiamine biosynthetic pathways (PubMed:12486071). It allows the use of exogenous aminoimidazole riboside (AIRs) to satisfy the cellular requirement for purines and thiamine (PubMed:12486071).[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
The crystal structures of a Salmonella enterica aminoimidazole riboside (AIRs) kinase, its complex with the substrate AIRs, and its complex with AIRs and an ATP analog were determined at 2.6 angstroms, 2.9 angstroms, and 2.7 angstroms, respectively. The product of the Salmonella-specific gene stm4066, AIRs kinase, is a homodimer with one active site per monomer. The core structure, consisting of an eight-stranded beta sheet flanked by eight alpha helices, indicates that AIRs kinase is a member of the ribokinase superfamily. Unlike ribokinase and adenosine kinase in this superfamily, AIRs kinase does not show significant conformational changes upon substrate binding. The active site is covered by a lid formed by residues 16-28 and 86-100. A comparison of the structure of AIRs kinase with other ribokinase superfamily members suggests that the active site lid and conformational changes that occur upon substrate binding may be advanced features in the evolution of the ribokinase superfamily.
Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily.,Zhang Y, Dougherty M, Downs DM, Ealick SE Structure. 2004 Oct;12(10):1809-21. PMID:15458630[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dougherty M, Downs DM. The stm4066 gene product of Salmonella enterica serovar Typhimurium has aminoimidazole riboside (AIRs) kinase activity and allows AIRs to satisfy the thiamine requirement of pur mutant strains. J Bacteriol. 2003 Jan;185(1):332-9. PMID:12486071 doi:10.1128/JB.185.1.332-339.2003
- ↑ Zhang Y, Dougherty M, Downs DM, Ealick SE. Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily. Structure. 2004 Oct;12(10):1809-21. PMID:15458630 doi:10.1016/j.str.2004.07.020
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