5fgw

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==Structure of Sda1 nuclease with bound zinc ion==
==Structure of Sda1 nuclease with bound zinc ion==
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<StructureSection load='5fgw' size='340' side='right' caption='[[5fgw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='5fgw' size='340' side='right'caption='[[5fgw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fgw]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FGW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fgw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FGW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fgu|5fgu]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=5fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgw OCA], [http://pdbe.org/5fgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fgw RCSB], [http://www.ebi.ac.uk/pdbsum/5fgw PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgw OCA], [https://pdbe.org/5fgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fgw RCSB], [https://www.ebi.ac.uk/pdbsum/5fgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgw ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q675N6_STRPY Q675N6_STRPY]
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Infection by Group A Streptococcus pyogenes (GAS) is a leading cause of severe invasive disease in humans, including streptococcal toxic shock syndrome and necrotizing fasciitis. GAS infections lead to nearly 163,000 annual deaths worldwide. Hypervirulent strains of S. pyogenes have evolved a plethora of virulence factors that aid in disease-by promoting bacterial adhesion to host cells, subsequent invasion of deeper tissues and blocking the immune system's attempts to eradicate the infection. Expression and secretion of the extracellular nuclease Sda1 is advantageous for promoting bacterial dissemination throughout the host organism, and evasion of the host's innate immune response. Here we present two crystal structures of Sda1, as well as biochemical studies to address key structural features and surface residues involved in DNA binding and catalysis. In the active site, Asn211 is observed to directly chelate a hydrated divalent metal ion and Arg124, on the putative substrate binding loop, likely stabilizes the transition state during phosphodiester bond cleavage. These structures provide a foundation for rational drug design of small molecule inhibitors to be used in prevention of invasive streptococcal disease.
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Structural characterization of the virulence factor Sda1 nuclease from Streptococcus pyogenes.,Moon AF, Krahn JM, Lu X, Cuneo MJ, Pedersen LC Nucleic Acids Res. 2016 May 5;44(8):3946-57. doi: 10.1093/nar/gkw143. Epub 2016, Mar 11. PMID:26969731<ref>PMID:26969731</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5fgw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cuneo, M J]]
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[[Category: Large Structures]]
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[[Category: Krahn, J M]]
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[[Category: Streptococcus pyogenes]]
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[[Category: Moon, A F]]
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[[Category: Cuneo MJ]]
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[[Category: Pedersen, L C]]
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[[Category: Krahn JM]]
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[[Category: Xun, L]]
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[[Category: Moon AF]]
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[[Category: Beta-beta-alpha metal finger nuclease]]
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[[Category: Pedersen LC]]
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[[Category: Dna binding protein]]
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[[Category: Xun L]]
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[[Category: Metal binding]]
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[[Category: Sequence nonspecific dna binding]]
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Current revision

Structure of Sda1 nuclease with bound zinc ion

PDB ID 5fgw

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