2xgr: Difference between revisions
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[[ | ==extracellular endonuclease== | ||
<StructureSection load='2xgr' size='340' side='right' caption='[[2xgr]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xgr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes_serotype_m1 Streptococcus pyogenes serotype m1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGR OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xgr RCSB], [http://www.ebi.ac.uk/pdbsum/2xgr PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The pathogenic bacterium Group A Streptococcus pyogenes produces several extracellular DNases that have been shown to facilitate invasive infection by evading the human host immune system. DNases degrade the chromatin in neutrophil extracellular traps, enabling the bacterium to evade neutrophil capture. Spd1 is a type I, nonspecific betabetaalpha/metal-dependent nuclease from Streptococcus pyogenes, which is encoded by the SF370.1 prophage and is likely to be expressed as a result of prophage induction. We present here the X-ray structure of this DNase in the wild-type and Asn145Ala mutant form. Through structural and sequence alignments as well as mutagenesis studies, we have identified the key residues His121, Asn145 and Glu164, which are crucial for Spd1 nucleolytic activity and shown the active site constellation. Our wild-type structure alludes to the possibility of a catalytically blocked dimeric form of the protein. We have investigated the multimeric nature of Spd1 using size-exclusion chromatography with multi-angle light scattering (SEC-MALLS) in the presence and absence of the divalent metal ion Mg(2+), which suggests that Spd1 exists in a monomeric form in solution. | |||
The structural characterization of a prophage-encoded extracellular DNase from Streptococcus pyogenes.,Korczynska JE, Turkenburg JP, Taylor EJ Nucleic Acids Res. 2011 Sep 24. PMID:21948797<ref>PMID:21948797</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Deoxyribonuclease I]] | [[Category: Deoxyribonuclease I]] | ||
[[Category: Streptococcus pyogenes serotype m1]] | [[Category: Streptococcus pyogenes serotype m1]] | ||
Revision as of 10:51, 14 May 2014
extracellular endonucleaseextracellular endonuclease
Structural highlights
Publication Abstract from PubMedThe pathogenic bacterium Group A Streptococcus pyogenes produces several extracellular DNases that have been shown to facilitate invasive infection by evading the human host immune system. DNases degrade the chromatin in neutrophil extracellular traps, enabling the bacterium to evade neutrophil capture. Spd1 is a type I, nonspecific betabetaalpha/metal-dependent nuclease from Streptococcus pyogenes, which is encoded by the SF370.1 prophage and is likely to be expressed as a result of prophage induction. We present here the X-ray structure of this DNase in the wild-type and Asn145Ala mutant form. Through structural and sequence alignments as well as mutagenesis studies, we have identified the key residues His121, Asn145 and Glu164, which are crucial for Spd1 nucleolytic activity and shown the active site constellation. Our wild-type structure alludes to the possibility of a catalytically blocked dimeric form of the protein. We have investigated the multimeric nature of Spd1 using size-exclusion chromatography with multi-angle light scattering (SEC-MALLS) in the presence and absence of the divalent metal ion Mg(2+), which suggests that Spd1 exists in a monomeric form in solution. The structural characterization of a prophage-encoded extracellular DNase from Streptococcus pyogenes.,Korczynska JE, Turkenburg JP, Taylor EJ Nucleic Acids Res. 2011 Sep 24. PMID:21948797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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