1tyy
From Proteopedia
(Difference between revisions)
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<StructureSection load='1tyy' size='340' side='right'caption='[[1tyy]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1tyy' size='340' side='right'caption='[[1tyy]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1tyy]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1tyy]] 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=1TYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYY FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1tyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyy OCA], [https://pdbe.org/1tyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tyy RCSB], [https://www.ebi.ac.uk/pdbsum/1tyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyy ProSAT]</span></td></tr> | |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tyy ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tyy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == 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<ref>PMID:15458630</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1tyy" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Fructokinase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
- | [[Category: Dougherty | + | [[Category: Dougherty M]] |
- | [[Category: Downs | + | [[Category: Downs DM]] |
- | [[Category: Ealick | + | [[Category: Ealick SE]] |
- | [[Category: Zhang | + | [[Category: Zhang Y]] |
- | + | ||
- | + | ||
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Revision as of 08:45, 1 May 2024
Crystal structure of aminoimidazole riboside kinase from Salmonella enterica
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