5a3a: Difference between revisions

Latest revision as of 11:36, 9 May 2024

Crystal structure of the ADP-ribosylating sirtuin (SirTM) from Streptococcus pyogenes (Apo form)

Structural highlights

5a3a is a 1 chain structure with sequence from Streptococcus pyogenes str. Manfredo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.54Å
Ligands:	EDO, GLY, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q1JGN6_STRPD

Publication Abstract from PubMed

Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species.

Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.,Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I Mol Cell. 2015 Jul 16;59(2):309-20. doi: 10.1016/j.molcel.2015.06.013. Epub 2015 , Jul 9. PMID:26166706^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Mol Cell. 2015 Jul 16;59(2):309-20. doi: 10.1016/j.molcel.2015.06.013. Epub 2015 , Jul 9. PMID:26166706 doi:https://dx.doi.org/10.1016/j.molcel.2015.06.013

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OCA

[1] Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Mol Cell. 2015 Jul 16;59(2):309-20. doi: 10.1016/j.molcel.2015.06.013. Epub 2015 , Jul 9. PMID:26166706 doi:https://dx.doi.org/10.1016/j.molcel.2015.06.013

[1]

@@ Line 1: / Line 1: @@
 ==Crystal structure of the ADP-ribosylating sirtuin (SirTM) from Streptococcus pyogenes (Apo form)==
-<StructureSection load='5a3a' size='340' side='right' caption='[[5a3a]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
+<StructureSection load='5a3a' size='340' side='right'caption='[[5a3a]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5a3a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A3A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5a3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_str._Manfredo Streptococcus pyogenes str. Manfredo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A3A FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</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]] 1.54&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a35|5a35]], [[5a3b|5a3b]], [[5a3c|5a3c]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=5a3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3a OCA], [https://pdbe.org/5a3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a3a RCSB], [https://www.ebi.ac.uk/pdbsum/5a3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3a ProSAT]</span></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=5a3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a3a RCSB], [http://www.ebi.ac.uk/pdbsum/5a3a PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q1JGN6_STRPD Q1JGN6_STRPD]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5a3a" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ahel, I]]
+[[Category: Large Structures]]
-[[Category: Ariza, A]]
+[[Category: Streptococcus pyogenes str. Manfredo]]
-[[Category: Barkauskaite, E]]
+[[Category: Ahel I]]
-[[Category: Cameron, D R]]
+[[Category: Ariza A]]
-[[Category: Kraehenbuehl, R]]
+[[Category: Barkauskaite E]]
-[[Category: Leidecker, O]]
+[[Category: Cameron DR]]
-[[Category: Leys, D]]
+[[Category: Kraehenbuehl R]]
-[[Category: Matic, I]]
+[[Category: Leidecker O]]
-[[Category: Morra, R]]
+[[Category: Leys D]]
-[[Category: Ortmayer, M]]
+[[Category: Matic I]]
-[[Category: Peleg, A Y]]
+[[Category: Morra R]]
-[[Category: Qu, Y]]
+[[Category: Ortmayer M]]
-[[Category: Rack, J G.M]]
+[[Category: Peleg AY]]
-[[Category: Traven, A]]
+[[Category: Qu Y]]
-[[Category: Lipoylation]]
+[[Category: Rack JGM]]
-[[Category: Metalloprotein]]
+[[Category: Traven A]]
-[[Category: Nad-dependent]]
-[[Category: P-ribosyltransferase]]
-[[Category: Regulatory enzyme]]
-[[Category: Ros defense]]
-[[Category: Rossmann fold]]
-[[Category: Transferase]]
-[[Category: Zinc binding]]

5a3a: Difference between revisions

Latest revision as of 11:36, 9 May 2024

Crystal structure of the ADP-ribosylating sirtuin (SirTM) from Streptococcus pyogenes (Apo form)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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