3ssc: Difference between revisions

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==DNA binding domain of restriction endonuclease bound to DNA==
==DNA binding domain of restriction endonuclease bound to DNA==
<StructureSection load='3ssc' size='340' side='right' caption='[[3ssc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3ssc' size='340' side='right'caption='[[3ssc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ssc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SSC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ssc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSC FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ssd|3ssd]], [[3sse|3sse]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ssd|3ssd]], [[3sse|3sse]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4346, JW5871, mcrB, rglB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4346, JW5871, mcrB, rglB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<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=3ssc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssc OCA], [http://pdbe.org/3ssc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ssc RCSB], [http://www.ebi.ac.uk/pdbsum/3ssc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssc ProSAT]</span></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=3ssc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssc OCA], [https://pdbe.org/3ssc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ssc RCSB], [https://www.ebi.ac.uk/pdbsum/3ssc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MCRB_ECOLI MCRB_ECOLI]] Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities.  
[[https://www.uniprot.org/uniprot/MCRB_ECOLI MCRB_ECOLI]] Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities.  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Grazulis, S]]
[[Category: Grazulis, S]]
[[Category: Siksnys, V]]
[[Category: Siksnys, V]]