View source for 4qgo


==Crystal structure of NucA from Streptococcus agalactiae with no metal bound==
<StructureSection load='4qgo' size='340' side='right'caption='[[4qgo]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qgo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_ILRI112 Streptococcus agalactiae ILRI112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QGO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4qgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qgo OCA], [https://pdbe.org/4qgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qgo RCSB], [https://www.ebi.ac.uk/pdbsum/4qgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qgo ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The group B pathogen Streptococcus agalactiae commonly populates the human gut and urogenital tract, and is a major cause of infection-based mortality in neonatal infants and in elderly or immunocompromised adults. Nuclease A (GBS_NucA), a secreted DNA/RNA nuclease, serves as a virulence factor for S. agalactiae, facilitating bacterial evasion of the human innate immune response. GBS_NucA efficiently degrades the DNA matrix component of neutrophil extracellular traps (NETs), which attempt to kill and clear invading bacteria during the early stages of infection. In order to better understand the mechanisms of DNA substrate binding and catalysis of GBS_NucA, the high-resolution structure of a catalytically inactive mutant (H148G) was solved by X-ray crystallography. Several mutants on the surface of GBS_NucA which might influence DNA substrate binding and catalysis were generated and evaluated using an imidazole chemical rescue technique. While several of these mutants severely inhibited nuclease activity, two mutants (K146R and Q183A) exhibited significantly increased activity. These structural and biochemical studies have greatly increased our understanding of the mechanism of action of GBS_NucA in bacterial virulence and may serve as a foundation for the structure-based drug design of antibacterial compounds targeted to S. agalactiae.

Structural characterization of the virulence factor nuclease A from Streptococcus agalactiae.,Moon AF, Gaudu P, Pedersen LC Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2937-49. doi:, 10.1107/S1399004714019725. Epub 2014 Oct 23. PMID:25372684<ref>PMID:25372684</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qgo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus agalactiae ILRI112]]
[[Category: Gaudu P]]
[[Category: Moon AF]]
[[Category: Pedersen LC]]