5kiv: Difference between revisions
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<StructureSection load='5kiv' size='340' side='right'caption='[[5kiv]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5kiv' size='340' side='right'caption='[[5kiv]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kiv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5kiv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KIV 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=EOH:ETHANOL'>EOH</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]] 1.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5kiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kiv OCA], [https://pdbe.org/5kiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kiv RCSB], [https://www.ebi.ac.uk/pdbsum/5kiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kiv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ADPRH_STAAN ADPRH_STAAN] Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the reponse to host-derived oxidative stress.[UniProtKB:P67343] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Appel CD]] | ||
[[Category: | [[Category: Feld GK]] | ||
[[Category: | [[Category: Wallace BD]] | ||
[[Category: | [[Category: Williams RS]] | ||
Latest revision as of 13:01, 27 September 2023
Crystal structure of SauMacro (SAV0325)Crystal structure of SauMacro (SAV0325)
Structural highlights
FunctionADPRH_STAAN Specifically reverses the SirTM-mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from the target protein. May be involved in the modulation of the reponse to host-derived oxidative stress.[UniProtKB:P67343] Publication Abstract from PubMedCells use the post-translational modification ADP-ribosylation to control a host of biological activities. In some pathogenic bacteria, an operon-encoded mono-ADP-ribosylation cycle mediates response to host-induced oxidative stress. In this system, reversible mono ADP-ribosylation of a lipoylated target protein represses oxidative stress response. An NAD+ -dependent sirtuin catalyzes the single ADP-ribose (ADPr) addition, while a linked macrodomain-containing protein removes the ADPr. Here we report the crystal structure of the sitruin-linked macrodomain protein from Staphylococcus aureus, SauMacro (also known as SAV0325) to 1.75-A resolution. The monomeric SauMacro bears a previously unidentified Zn2+ -binding site that putatively aids in substrate recognition and catalysis. An amino-terminal three-helix bundle motif unique to this class of macrodomain proteins provides a structural scaffold for the Zn2+ site. Structural features of the enzyme further indicate a cleft proximal to the Zn2+ binding site appears well suited for ADPr binding, while a deep hydrophobic channel in the protein core is suitable for binding the lipoate of the lipoylated protein target. Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureus.,Appel CD, Feld GK, Wallace BD, Williams RS Protein Sci. 2016 Jun 27. doi: 10.1002/pro.2974. PMID:27345688[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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