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| | ==Crystal structure of pppGpp bound RbgA from S. aureus== | | ==Crystal structure of pppGpp bound RbgA from S. aureus== |
| - | <StructureSection load='6g15' size='340' side='right' caption='[[6g15]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='6g15' size='340' side='right'caption='[[6g15]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6g15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa3 Staa3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G15 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_USA300 Staphylococcus aureus subsp. aureus USA300]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G15 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1Z:guanosine+3-diphosphate+5-triphosphate'>C1Z</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]] 1.65Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAUSA300_1136 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367830 STAA3])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1Z:guanosine+3-diphosphate+5-triphosphate'>C1Z</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6g15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g15 OCA], [http://pdbe.org/6g15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g15 RCSB], [http://www.ebi.ac.uk/pdbsum/6g15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g15 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=6g15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g15 OCA], [https://pdbe.org/6g15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g15 RCSB], [https://www.ebi.ac.uk/pdbsum/6g15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g15 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0H2XK72_STAA3 A0A0H2XK72_STAA3]] Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.[PIRNR:PIRNR006230] | + | [https://www.uniprot.org/uniprot/A0A0H2XK72_STAA3 A0A0H2XK72_STAA3] Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.[PIRNR:PIRNR006230] |
| | <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: Staa3]] | + | [[Category: Large Structures]] |
| - | [[Category: Bange, G]] | + | [[Category: Staphylococcus aureus subsp. aureus USA300]] |
| - | [[Category: Pausch, P]] | + | [[Category: Bange G]] |
| - | [[Category: Cpgtpase]] | + | [[Category: Pausch P]] |
| - | [[Category: Rna binding protein]]
| + | |
| Structural highlights
Function
A0A0H2XK72_STAA3 Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.[PIRNR:PIRNR006230]
Publication Abstract from PubMed
Efficient adaptation to environmental changes is pivotal for all bacterial cells. Almost all bacterial species depend on the conserved stringent response system to prompt timely transcriptional and metabolic responses according to stress conditions and nutrient depletion. The stringent response relies on the stress-dependent synthesis of the second messenger nucleotides and alarmones (p)ppGpp, which pleiotropically target and reprogram processes that consume cellular resources, such as ribosome biogenesis. Here we show that (p)ppGpp acts on the ribosome biogenesis GTPase A (RbgA) of Gram-positive bacteria. Using X-ray crystallography, hydrogen-deuterium exchange mass spectrometry (HDX-MS) and kinetic analysis, we demonstrate that the alarmones (p)ppGpp bind to RbgA in a manner similar to that of binding by GDP and GTP and therby act as competitive inhibitors. Our structural analysis of Staphylococcus aureus RbgA bound to ppGpp and pppGpp at 1.8 A and 1.65 A resolution, respectively, suggested that the alarmones (p)ppGpp prevent the active GTPase conformation of RbgA by sterically blocking the association of its G2 motif via their 3'-pyrophosphate moieties. Taken together, our structural and biochemical characterization of RbgA in the context of the alarmone-mediated stringent response reveals how (p)ppGpp affects the function of RbgA and reprograms this GTPase to arrest the ribosomal large subunit.
Structural basis for (p)ppGpp-mediated inhibition of the GTPase RbgA.,Pausch P, Steinchen W, Wieland M, Klaus T, Freibert SA, Altegoer F, Wilson DN, Bange G J Biol Chem. 2018 Oct 26. pii: RA118.003070. doi: 10.1074/jbc.RA118.003070. PMID:30366986[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pausch P, Steinchen W, Wieland M, Klaus T, Freibert SA, Altegoer F, Wilson DN, Bange G. Structural basis for (p)ppGpp-mediated inhibition of the GTPase RbgA. J Biol Chem. 2018 Oct 26. pii: RA118.003070. doi: 10.1074/jbc.RA118.003070. PMID:30366986 doi:http://dx.doi.org/10.1074/jbc.RA118.003070
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