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3owv

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Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae

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 <StructureSection load='3owv' size='340' side='right'caption='[[3owv]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3owv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3owv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWV FirstGlance]. <br>
-</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=MG:MAGNESIUM+ION'>MG</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]] 1.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g8t|1g8t]], [[1zm8|1zm8]], [[3ism|3ism]], [[1oup|1oup]]</div></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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">endA, SP_1964 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</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=3owv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3owv OCA], [https://pdbe.org/3owv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3owv RCSB], [https://www.ebi.ac.uk/pdbsum/3owv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3owv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/NUCE_STRPN NUCE_STRPN]] By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed.
+[https://www.uniprot.org/uniprot/NUCE_STRPN NUCE_STRPN] By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-EndA is a sequence non-specific endonuclease that serves as a virulence factor during Streptococcus pneumoniae infection. Expression of EndA provides a strategy for evasion of the host's neutrophil extracellular traps, digesting the DNA scaffold structure and allowing further invasion by S. pneumoniae. To define mechanisms of catalysis and substrate binding, we solved the structure of EndA at 1.75 A resolution. The EndA structure reveals a DRGH (Asp-Arg-Gly-His) motif-containing betabetaalpha-metal finger catalytic core augmented by an interesting 'finger-loop' interruption of the active site alpha-helix. Subsequently, we delineated DNA binding versus catalytic functionality using structure-based alanine substitution mutagenesis. Three mutants, H154A, Q186A and Q192A, exhibited decreased nuclease activity that appears to be independent of substrate binding. Glu205 was found to be crucial for catalysis, while residues Arg127/Lys128 and Arg209/Lys210 contribute to substrate binding. The results presented here provide the molecular foundation for development of specific antibiotic inhibitors for EndA.
-Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae.,Moon AF, Midon M, Meiss G, Pingoud A, London RE, Pedersen LC Nucleic Acids Res. 2010 Nov 26. PMID:21113026<ref>PMID:21113026</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3owv" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: London, R E]]
+[[Category: Streptococcus pneumoniae]]
-[[Category: Meiss, G]]
+[[Category: London RE]]
-[[Category: Midon, M]]
+[[Category: Meiss G]]
-[[Category: Moon, A F]]
+[[Category: Midon M]]
-[[Category: Pedersen, L C]]
+[[Category: Moon AF]]
-[[Category: Pingoud, A M]]
+[[Category: Pedersen LC]]
-[[Category: Hydrolase]]
+[[Category: Pingoud AM]]
-[[Category: Sequence nonspecific endonuclease]]

3owv

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Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae

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