3rec

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[[Image:3rec.gif|left|200px]]
 
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==ESCHERICHIA COLI RECA PROTEIN-BOUND DNA, NMR, 1 STRUCTURE==
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The line below this paragraph, containing "STRUCTURE_3rec", creates the "Structure Box" on the page.
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<StructureSection load='3rec' size='340' side='right'caption='[[3rec]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3rec]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3REC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=3rec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rec OCA], [https://pdbe.org/3rec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rec RCSB], [https://www.ebi.ac.uk/pdbsum/3rec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rec ProSAT]</span></td></tr>
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{{STRUCTURE_3rec| PDB=3rec | SCENE= }}
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</table>
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<div style="background-color:#fffaf0;">
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'''ESCHERICHIA COLI RECA PROTEIN-BOUND DNA, NMR, 1 STRUCTURE'''
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== Publication Abstract from PubMed ==
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==Overview==
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The family of proteins that are homologous to RecA protein of Escherichia coli is essential to homologous genetic recombination in various organisms including viruses, bacteria, lower eukaryotes, and mammals. In the presence of ATP (or ATPgammaS), these proteins form helical filaments containing single-stranded DNA at the center. The single-stranded DNA bound to RecA protein is extended 1.5 times relative to B-form DNA with the same sequence, and the extension is critical to pairing with homologous double-stranded DNA. This pairing reaction, called homologous pairing, is a key reaction in homologous recombination. In this NMR study, we determined a three-dimensional structure of the single-stranded DNA bound to RecA protein. The DNA structure contains novel deoxyribose-base stacking in which the 2'-methylene moiety of each deoxyribose is placed above the base of the following residue, instead of normal stacking of adjacent bases. As a result of this deoxyribose-base stacking, bases of the single-stranded DNA are spaced out nearly 5 A. Thus, this novel structure well explains the axial extension of DNA in the RecA-filaments relative to B-form DNA and leads to a possible interpretation of the role of this extension in homologous pairing.
The family of proteins that are homologous to RecA protein of Escherichia coli is essential to homologous genetic recombination in various organisms including viruses, bacteria, lower eukaryotes, and mammals. In the presence of ATP (or ATPgammaS), these proteins form helical filaments containing single-stranded DNA at the center. The single-stranded DNA bound to RecA protein is extended 1.5 times relative to B-form DNA with the same sequence, and the extension is critical to pairing with homologous double-stranded DNA. This pairing reaction, called homologous pairing, is a key reaction in homologous recombination. In this NMR study, we determined a three-dimensional structure of the single-stranded DNA bound to RecA protein. The DNA structure contains novel deoxyribose-base stacking in which the 2'-methylene moiety of each deoxyribose is placed above the base of the following residue, instead of normal stacking of adjacent bases. As a result of this deoxyribose-base stacking, bases of the single-stranded DNA are spaced out nearly 5 A. Thus, this novel structure well explains the axial extension of DNA in the RecA-filaments relative to B-form DNA and leads to a possible interpretation of the role of this extension in homologous pairing.
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==About this Structure==
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An extended DNA structure through deoxyribose-base stacking induced by RecA protein.,Nishinaka T, Ito Y, Yokoyama S, Shibata T Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6623-8. PMID:9192615<ref>PMID:9192615</ref>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3REC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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An extended DNA structure through deoxyribose-base stacking induced by RecA protein., Nishinaka T, Ito Y, Yokoyama S, Shibata T, Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6623-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9192615 9192615]
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</div>
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[[Category: Ito, Y.]]
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<div class="pdbe-citations 3rec" style="background-color:#fffaf0;"></div>
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[[Category: Nishinaka, T.]]
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== References ==
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[[Category: Shibata, T.]]
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<references/>
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[[Category: Yokoyama, S.]]
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__TOC__
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[[Category: Deoxyribonucleic acid]]
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</StructureSection>
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[[Category: Deoxyribose-base stacking]]
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[[Category: Large Structures]]
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[[Category: Homologous pairing]]
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[[Category: Ito Y]]
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[[Category: Homologous recombination]]
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[[Category: Nishinaka T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:58:33 2008''
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[[Category: Shibata T]]
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[[Category: Yokoyama S]]

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ESCHERICHIA COLI RECA PROTEIN-BOUND DNA, NMR, 1 STRUCTURE

PDB ID 3rec

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