3rec
From Proteopedia
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| - | + | ==ESCHERICHIA COLI RECA PROTEIN-BOUND DNA, NMR, 1 STRUCTURE== | |
| - | + | <StructureSection load='3rec' size='340' side='right' caption='[[3rec]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3REC FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ew1|1ew1]]</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=3rec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rec RCSB], [http://www.ebi.ac.uk/pdbsum/3rec PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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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| - | [[Category: Ito, Y | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Nishinaka, T | + | </div> |
| - | [[Category: Shibata, T | + | |
| - | [[Category: Yokoyama, S | + | ==See Also== |
| + | *[[Antimicrobial peptides|Antimicrobial peptides]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ito, Y]] | ||
| + | [[Category: Nishinaka, T]] | ||
| + | [[Category: Shibata, T]] | ||
| + | [[Category: Yokoyama, S]] | ||
[[Category: Deoxyribonucleic acid]] | [[Category: Deoxyribonucleic acid]] | ||
[[Category: Deoxyribose-base stacking]] | [[Category: Deoxyribose-base stacking]] | ||
Revision as of 12:39, 5 January 2015
ESCHERICHIA COLI RECA PROTEIN-BOUND DNA, NMR, 1 STRUCTURE
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