4beb

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(New page: '''Unreleased structure''' The entry 4beb is ON HOLD Authors: Csefalvay, E., Lapkouski, M., Guzanova, A., Csefalvay, L., Baikova, T., Shevelev, I., Janscak, P., Smatanova, I.K., Panjika...)
Current revision (11:49, 20 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4beb is ON HOLD
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==MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP==
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<StructureSection load='4beb' size='340' side='right'caption='[[4beb]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4beb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2y3t 2y3t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BEB FirstGlance]. <br>
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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]] 2.989&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4beb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4beb OCA], [https://pdbe.org/4beb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4beb RCSB], [https://www.ebi.ac.uk/pdbsum/4beb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4beb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/T1R1_ECOLX T1R1_ECOLX] The restriction (R) subunit of a type I restriction enzyme that recognizes 5'-GAAN(7)RTCG-3' and cleaves a random distance away. Subunit R is required for both nuclease and ATPase activities, but not for modification (Probable) (PubMed:12654995). After locating an unmethylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (Probable). The enzyme undergoes major structural changes to bring the motor domains into contact with DNA, allowing DNA translocation. This prevents DNA access to the catalytic domains of both the R and M subunits, preventing both restriction and methylation (PubMed:32483229).<ref>PMID:32483229</ref> <ref>PMID:12654995</ref> <ref>PMID:2784505</ref> <ref>PMID:32483229</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of the Type I restriction systems that is consistent with their proposed role in horizontal gene transfer. DNA cleavage occurs at nonspecific sites distant from the cognate recognition sequence, apparently triggered by stalled translocation. The X-ray crystal structure of the complete HsdR subunit from E. coli plasmid R124 suggested that the triggering mechanism involves interdomain contacts mediated by ATP. In the present work, in vivo and in vitro activity assays and crystal structures of three mutants of EcoR124I HsdR designed to probe this mechanism are reported. The results indicate that interdomain engagement via ATP is indeed responsible for signal transmission between the endonuclease and helicase domains of the motor subunit. A previously identified sequence motif that is shared by the RecB nucleases and some Type I endonucleases is implicated in signaling.
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Authors: Csefalvay, E., Lapkouski, M., Guzanova, A., Csefalvay, L., Baikova, T., Shevelev, I., Janscak, P., Smatanova, I.K., Panjikar, S., Carey, J., Weiserova, M., Ettrich, R.
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Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.,Csefalvay E, Lapkouski M, Guzanova A, Csefalvay L, Baikova T, Shevelev I, Bialevich V, Shamayeva K, Janscak P, Kuta Smatanova I, Panjikar S, Carey J, Weiserova M, Ettrich R PLoS One. 2015 Jun 3;10(6):e0128700. doi: 10.1371/journal.pone.0128700., eCollection 2015. PMID:26039067<ref>PMID:26039067</ref>
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Description: MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4beb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Baikova T]]
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[[Category: Carey J]]
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[[Category: Csefalvay E]]
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[[Category: Csefalvay L]]
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[[Category: Ettrich R]]
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[[Category: Guzanova A]]
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[[Category: Janscak P]]
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[[Category: Lapkouski M]]
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[[Category: Panjikar S]]
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[[Category: Shevelev I]]
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[[Category: Smatanova IK]]
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[[Category: Weiserova M]]

Current revision

MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP

PDB ID 4beb

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