1fu1

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(New page: 200px<br /> <applet load="1fu1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fu1, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1fu1, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN XRCC4'''<br />
'''CRYSTAL STRUCTURE OF HUMAN XRCC4'''<br />
==Overview==
==Overview==
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XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ), in all eukaryotes and, in particular, V(D)J recombination in vertebrates., Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends, in the last step of V(D)J recombination and NHEJ to repair double strand, breaks. XRCC4-defective cells are extremely sensitive to ionizing, radiation, and disruption of the XRCC4 gene results in embryonic lethality, in mice. Here we report the crystal structure of a functional fragment of, Xrcc4 at 2.7 A resolution. Xrcc4 protein forms a strikingly elongated, dumb-bell-like tetramer. Each of the N-terminal globular head domains, consists of a beta-sandwich and a potentially DNA-binding helix-, turn-helix motif. The C-terminal stalk comprising a single alpha-helix, &gt;120 A in length is partly incorporated into a four-helix bundle in the, Xrcc4 tetramer and partly involved in interacting with ligase IV. The, Xrcc4 structure suggests a possible mode of coupling ligase IV association, with DNA binding for effective ligation of DNA ends.
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XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ) in all eukaryotes and, in particular, V(D)J recombination in vertebrates. Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends in the last step of V(D)J recombination and NHEJ to repair double strand breaks. XRCC4-defective cells are extremely sensitive to ionizing radiation, and disruption of the XRCC4 gene results in embryonic lethality in mice. Here we report the crystal structure of a functional fragment of Xrcc4 at 2.7 A resolution. Xrcc4 protein forms a strikingly elongated dumb-bell-like tetramer. Each of the N-terminal globular head domains consists of a beta-sandwich and a potentially DNA-binding helix- turn-helix motif. The C-terminal stalk comprising a single alpha-helix &gt;120 A in length is partly incorporated into a four-helix bundle in the Xrcc4 tetramer and partly involved in interacting with ligase IV. The Xrcc4 structure suggests a possible mode of coupling ligase IV association with DNA binding for effective ligation of DNA ends.
==About this Structure==
==About this Structure==
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1FU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FU1 OCA].
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1FU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FU1 OCA].
==Reference==
==Reference==
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[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:57:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:38 2008''

Revision as of 10:42, 21 February 2008

Image:1fu1.gif

1fu1, resolution 2.70Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF HUMAN XRCC4

Overview

XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ) in all eukaryotes and, in particular, V(D)J recombination in vertebrates. Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends in the last step of V(D)J recombination and NHEJ to repair double strand breaks. XRCC4-defective cells are extremely sensitive to ionizing radiation, and disruption of the XRCC4 gene results in embryonic lethality in mice. Here we report the crystal structure of a functional fragment of Xrcc4 at 2.7 A resolution. Xrcc4 protein forms a strikingly elongated dumb-bell-like tetramer. Each of the N-terminal globular head domains consists of a beta-sandwich and a potentially DNA-binding helix- turn-helix motif. The C-terminal stalk comprising a single alpha-helix >120 A in length is partly incorporated into a four-helix bundle in the Xrcc4 tetramer and partly involved in interacting with ligase IV. The Xrcc4 structure suggests a possible mode of coupling ligase IV association with DNA binding for effective ligation of DNA ends.

About this Structure

1FU1 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Xrcc4 DNA repair protein and implications for end joining., Junop MS, Modesti M, Guarne A, Ghirlando R, Gellert M, Yang W, EMBO J. 2000 Nov 15;19(22):5962-70. PMID:11080143

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