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2w35

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Current revision (05:49, 5 July 2023) (edit) (undo)
 
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<StructureSection load='2w35' size='340' side='right'caption='[[2w35]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='2w35' size='340' side='right'caption='[[2w35]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2w35]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W35 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2w35]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W35 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DI:2-DEOXYINOSINE-5-MONOPHOSPHATE'>DI</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2w36|2w36]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxyribonuclease_V Deoxyribonuclease V], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.7 3.1.21.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w35 OCA], [https://pdbe.org/2w35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w35 RCSB], [https://www.ebi.ac.uk/pdbsum/2w35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w35 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=2w35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w35 OCA], [https://pdbe.org/2w35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w35 RCSB], [https://www.ebi.ac.uk/pdbsum/2w35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w35 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA]] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref>
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[https://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
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[[Category: Deoxyribonuclease V]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alseth, I]]
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[[Category: Thermotoga maritima]]
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[[Category: Arvai, A S]]
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[[Category: Alseth I]]
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[[Category: Backe, P H]]
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[[Category: Arvai AS]]
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[[Category: Bjoras, M]]
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[[Category: Backe PH]]
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[[Category: Cao, W]]
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[[Category: Bjoras M]]
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[[Category: Dalhus, B]]
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[[Category: Cao W]]
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[[Category: Gao, H]]
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[[Category: Dalhus B]]
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[[Category: Olsen, O E]]
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[[Category: Gao H]]
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[[Category: Rosnes, I]]
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[[Category: Olsen OE]]
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[[Category: Tainer, J A]]
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[[Category: Rosnes I]]
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[[Category: Dna damage]]
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[[Category: Tainer JA]]
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[[Category: Dna repair]]
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[[Category: Endonuclease]]
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[[Category: Endonucleasev]]
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[[Category: Hydrolase]]
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[[Category: Hypoxanthine]]
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[[Category: Inosine]]
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Current revision

Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair

PDB ID 2w35

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