4ceh

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m (Protected "4ceh" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4ceh| PDB=4ceh | SCENE= }}
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===Crystal structure of AddAB with a forked DNA substrate===
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The entry 4ceh is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/ADDA_BACSU ADDA_BACSU]] An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.<ref>PMID:8387145</ref> <ref>PMID:10756102</ref> <ref>PMID:17570399</ref> [[http://www.uniprot.org/uniprot/ADDB_BACSU ADDB_BACSU]] The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent single-stranded exonuclease, acting in both directions. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' to 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.<ref>PMID:8387145</ref> <ref>PMID:10756102</ref> <ref>PMID:17570399</ref>
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Authors: Krajewski, W.W., Wilkinson, M., Fu, X., Cronin, N.B., Wigley, D.
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==About this Structure==
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[[4ceh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CEH OCA].
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Description: Crystal structure of AddAB with a forked DNA substrate
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Cronin, N B.]]
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[[Category: Fu, X.]]
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[[Category: Krajewski, W W.]]
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[[Category: Wigley, D.]]
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[[Category: Wilkinson, M.]]
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[[Category: Bacterial protein]]
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[[Category: Binding site]]
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[[Category: Dna break]]
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[[Category: Dna helicase]]
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[[Category: Dna repair]]
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[[Category: Dna- binding protein]]
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[[Category: Double-stranded]]
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[[Category: Exodeoxyribonuclease v]]
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[[Category: Exodeoxyribonuclease]]
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[[Category: Helicase-nuclease]]
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[[Category: Homologous recombination]]
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[[Category: Hydrolase-dna complex]]

Revision as of 13:55, 12 March 2014

Template:STRUCTURE 4ceh

Contents

Crystal structure of AddAB with a forked DNA substrate

Function

[ADDA_BACSU] An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.[1] [2] [3] [ADDB_BACSU] The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent single-stranded exonuclease, acting in both directions. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' to 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.[4] [5] [6]

About this Structure

4ceh is a 3 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Kooistra J, Haijema BJ, Venema G. The Bacillus subtilis addAB genes are fully functional in Escherichia coli. Mol Microbiol. 1993 Mar;7(6):915-23. PMID:8387145
  2. ↑ Chedin F, Ehrlich SD, Kowalczykowski SC. The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro. J Mol Biol. 2000 Apr 21;298(1):7-20. PMID:10756102 doi:http://dx.doi.org/10.1006/jmbi.2000.3556
  3. ↑ Yeeles JT, Dillingham MS. A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases. J Mol Biol. 2007 Aug 3;371(1):66-78. Epub 2007 May 25. PMID:17570399 doi:http://dx.doi.org/10.1016/j.jmb.2007.05.053
  4. ↑ Kooistra J, Haijema BJ, Venema G. The Bacillus subtilis addAB genes are fully functional in Escherichia coli. Mol Microbiol. 1993 Mar;7(6):915-23. PMID:8387145
  5. ↑ Chedin F, Ehrlich SD, Kowalczykowski SC. The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro. J Mol Biol. 2000 Apr 21;298(1):7-20. PMID:10756102 doi:http://dx.doi.org/10.1006/jmbi.2000.3556
  6. ↑ Yeeles JT, Dillingham MS. A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases. J Mol Biol. 2007 Aug 3;371(1):66-78. Epub 2007 May 25. PMID:17570399 doi:http://dx.doi.org/10.1016/j.jmb.2007.05.053

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