3orq: Difference between revisions
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==Crystal Structure of N5-Carboxyaminoimidazole synthetase from Staphylococcus aureus complexed with ADP== | ==Crystal Structure of N5-Carboxyaminoimidazole synthetase from Staphylococcus aureus complexed with ADP== | ||
<StructureSection load='3orq' size='340' side='right' caption='[[3orq]], [[Resolution|resolution]] 2.23Å' scene=''> | <StructureSection load='3orq' size='340' side='right'caption='[[3orq]], [[Resolution|resolution]] 2.23Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3orq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3orq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_str._Newman Staphylococcus aureus subsp. aureus str. Newman]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ORQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ORQ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | |||
<tr | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3orq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3orq OCA], [https://pdbe.org/3orq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3orq RCSB], [https://www.ebi.ac.uk/pdbsum/3orq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3orq ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H3KFM7_STAAE A0A0H3KFM7_STAAE] Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).[HAMAP-Rule:MF_01928] Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).[RuleBase:RU361200] | |||
<table> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structural and biochemical characterization of N5-carboxyaminoimidazole ribonucleotide synthetase and N5-carboxyaminoimidazole ribonucleotide mutase from Staphylococcus aureus.,Brugarolas P, Duguid EM, Zhang W, Poor CB, He C Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):707-15. Epub 2011 Jul 12. PMID:21795812<ref>PMID:21795812</ref> | Structural and biochemical characterization of N5-carboxyaminoimidazole ribonucleotide synthetase and N5-carboxyaminoimidazole ribonucleotide mutase from Staphylococcus aureus.,Brugarolas P, Duguid EM, Zhang W, Poor CB, He C Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):707-15. Epub 2011 Jul 12. PMID:21795812<ref>PMID:21795812</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3orq" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphoribosylaminoimidazole carboxylase 3D structures|Phosphoribosylaminoimidazole carboxylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Staphylococcus aureus subsp. aureus]] | [[Category: Large Structures]] | ||
[[Category: Brugarolas | [[Category: Staphylococcus aureus subsp. aureus str. Newman]] | ||
[[Category: Duguid | [[Category: Brugarolas P]] | ||
[[Category: He | [[Category: Duguid EM]] | ||
[[Category: Poor | [[Category: He C]] | ||
[[Category: Zhang | [[Category: Poor CB]] | ||
[[Category: Zhang W]] | |||
Latest revision as of 13:17, 6 November 2024
Crystal Structure of N5-Carboxyaminoimidazole synthetase from Staphylococcus aureus complexed with ADPCrystal Structure of N5-Carboxyaminoimidazole synthetase from Staphylococcus aureus complexed with ADP
Structural highlights
FunctionA0A0H3KFM7_STAAE Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).[HAMAP-Rule:MF_01928] Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).[RuleBase:RU361200] Publication Abstract from PubMedWith the rapid rise of methicillin-resistant Staphylococcus aureus infections, new strategies against S. aureus are urgently needed. De novo purine biosynthesis is a promising yet unexploited target, insofar as abundant evidence has shown that bacteria with compromised purine biosynthesis are attenuated. Fundamental differences exist within the process by which humans and bacteria convert 5-aminoimidazole ribonucleotide (AIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). In bacteria, this transformation occurs through a two-step conversion catalyzed by PurK and PurE; in humans, it is mediated by a one-step conversion catalyzed by class II PurE. Thus, these bacterial enzymes are potential targets for selective antibiotic development. Here, the first comprehensive structural and biochemical characterization of PurK and PurE from S. aureus is presented. Structural analysis of S. aureus PurK reveals a nonconserved phenylalanine near the AIR-binding site that occupies the putative position of the imidazole ring of AIR. Mutation of this phenylalanine to isoleucine or tryptophan reduced the enzyme efficiency by around tenfold. The K(m) for bicarbonate was determined for the first time for a PurK enzyme and was found to be approximately 18.8 mM. The structure of PurE is described in comparison to that of human class II PurE. It is confirmed biochemically that His38 is essential for function. These studies aim to provide foundations for future structure-based drug-discovery efforts against S. aureus purine biosynthesis. Structural and biochemical characterization of N5-carboxyaminoimidazole ribonucleotide synthetase and N5-carboxyaminoimidazole ribonucleotide mutase from Staphylococcus aureus.,Brugarolas P, Duguid EM, Zhang W, Poor CB, He C Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):707-15. Epub 2011 Jul 12. PMID:21795812[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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