1ew1
From Proteopedia
(New page: 200px<br /><applet load="1ew1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ew1" /> '''RECA PROTEIN-BOUND SINGLE-STRANDED DNA'''<br...) |
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| - | [[Image:1ew1.gif|left|200px]]<br /><applet load="1ew1" size=" | + | [[Image:1ew1.gif|left|200px]]<br /><applet load="1ew1" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''RECA PROTEIN-BOUND SINGLE-STRANDED DNA'''<br /> | '''RECA PROTEIN-BOUND SINGLE-STRANDED DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The family of proteins that are homologous to RecA protein of Escherichia | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EW1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1EW1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EW1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: single-stranded dna]] | [[Category: single-stranded dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:12 2008'' |
Revision as of 10:32, 21 February 2008
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RECA PROTEIN-BOUND SINGLE-STRANDED DNA
Overview
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.
About this Structure
1EW1 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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