1kn0: Difference between revisions

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[[Image:1kn0.gif|left|200px]]<br />

[[Image:1kn0.gif|left|200px]]<br /><applet load="1kn0" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1kn0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1kn0, resolution 2.85Å" />

'''Crystal Structure of the human Rad52 protein'''<br />

==Overview==

The human Rad52 protein forms a heptameric ring that catalyzes homologous, pairing. The N-terminal half of Rad52 is the catalytic domain for, homologous pairing, and the ring formed by the domain fragment was, reported to be approximately decameric. Splicing variants of Rad52 and a, yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of, human Rad52 and revealed that the domain forms an undecameric ring. Each, monomer has a beta-beta-beta-alpha fold, which consists of highly, conserved amino acid residues among Rad52 homologs. A mutational analysis, revealed that the amino acid residues located between the, beta-beta-beta-alpha fold and the characteristic hairpin loop are, essential for ssDNA and dsDNA binding.

The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.

==About this Structure==

1KN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA].

1KN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA].

==Reference==

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[[Category: Kurumizaka, H.]]

[[Category: Nureki, O.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Shibata, T.]]

[[Category: Yokoyama, S.]]

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[[Category: structural genomics]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:52:~~46 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:54 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1kn0.gif|left|200px]]<br />
+[[Image:1kn0.gif|left|200px]]<br /><applet load="1kn0" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1kn0" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1kn0, resolution 2.85&Aring;" />
 '''Crystal Structure of the human Rad52 protein'''<br />
 ==Overview==
-The human Rad52 protein forms a heptameric ring that catalyzes homologous, pairing. The N-terminal half of Rad52 is the catalytic domain for, homologous pairing, and the ring formed by the domain fragment was, reported to be approximately decameric. Splicing variants of Rad52 and a, yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of, human Rad52 and revealed that the domain forms an undecameric ring. Each, monomer has a beta-beta-beta-alpha fold, which consists of highly, conserved amino acid residues among Rad52 homologs. A mutational analysis, revealed that the amino acid residues located between the, beta-beta-beta-alpha fold and the characteristic hairpin loop are, essential for ssDNA and dsDNA binding.
+The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
 ==About this Structure==
-KN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA].
+KN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN0 OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: Kurumizaka, H.]]
 [[Category: Nureki, O.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Shibata, T.]]
 [[Category: Yokoyama, S.]]
@@ Line 29: / Line 28: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:52:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:54 2008''