6yex

<StructureSection load='6yex' size='340' side='right'caption='[[6yex]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[6yex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25920 Atcc 25920]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YEX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YEX 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=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yex OCA], [http://pdbe.org/6yex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yex RCSB], [http://www.ebi.ac.uk/pdbsum/6yex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yex ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Modification dependent restriction endonucleases (MDREs) often have separate catalytic and modification dependent domains. We systematically looked for previously uncharacterized fusion proteins featuring a PUA or DUF3427 domain and HNH or PD-(D/E)XK catalytic domain. The enzymes were clustered by similarity of their putative modification sensing domains into several groups. The TspA15I (VcaM4I, CmeDI), ScoA3IV (MsiJI, VcaCI) and YenY4I groups, all featuring a PUA superfamily domain, preferentially cleaved DNA containing 5-methylcytosine or 5-hydroxymethylcytosine. ScoA3V, also featuring a PUA superfamily domain, but of a different clade, exhibited 6-methyladenine stimulated nicking activity. With few exceptions, ORFs for PUA-superfamily domain containing endonucleases were not close to DNA methyltransferase ORFs, strongly supporting modification dependent activity of the endonucleases. DUF3427 domain containing fusion proteins had very little or no endonuclease activity, despite the presence of a putative PD-(D/E)XK catalytic domain. However, their expression potently restricted phage T4gt in Escherichia coli cells. In contrast to the ORFs for PUA domain containing endonucleases, the ORFs for DUF3427 fusion proteins were frequently found in defense islands, often also featuring DNA methyltransferases.

A protein architecture guided screen for modification dependent restriction endonucleases.,Lutz T, Flodman K, Copelas A, Czapinska H, Mabuchi M, Fomenkov A, He X, Bochtler M, Xu SY Nucleic Acids Res. 2019 Oct 10;47(18):9761-9776. doi: 10.1093/nar/gkz755. PMID:31504772<ref>PMID:31504772</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 6yex" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 25920]]

[[Category: Bochtler, M]]

[[Category: Czapinska, H]]

[[Category: Helbrecht, I]]

[[Category: Lutz, T]]

[[Category: Pastor, M]]

[[Category: Xu, S]]

[[Category: Single stranded dna]]