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5kiv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of SauMacro (SAV0325)== | |
| + | <StructureSection load='5kiv' size='340' side='right' caption='[[5kiv]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5kiv]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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=5kiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kiv OCA], [http://pdbe.org/5kiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kiv RCSB], [http://www.ebi.ac.uk/pdbsum/5kiv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kiv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cells 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<ref>PMID:27345688</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Appel, C | + | <div class="pdbe-citations 5kiv" style="background-color:#fffaf0;"></div> |
| - | [[Category: Feld, G | + | == References == |
| - | [[Category: Wallace, B | + | <references/> |
| - | [[Category: Williams, R | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Appel, C D]] | ||
| + | [[Category: Feld, G K]] | ||
| + | [[Category: Wallace, B D]] | ||
| + | [[Category: Williams, R S]] | ||
| + | [[Category: Adp-ribose]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Lipoate binding]] | ||
| + | [[Category: Macrodomain]] | ||
| + | [[Category: Zn binding]] | ||
Revision as of 11:50, 14 July 2016
Crystal structure of SauMacro (SAV0325)
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