4ceh: Difference between revisions
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{{STRUCTURE_4ceh| PDB=4ceh | SCENE= }} | |||
===Crystal structure of AddAB with a forked DNA substrate=== | |||
The | ==Function== | ||
[[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> | |||
==About this Structure== | |||
[[4ceh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CEH OCA]. | |||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Cronin, N B.]] | |||
[[Category: Fu, X.]] | |||
[[Category: Krajewski, W W.]] | |||
[[Category: Wigley, D.]] | |||
[[Category: Wilkinson, M.]] | |||
[[Category: Bacterial protein]] | |||
[[Category: Binding site]] | |||
[[Category: Dna break]] | |||
[[Category: Dna helicase]] | |||
[[Category: Dna repair]] | |||
[[Category: Dna- binding protein]] | |||
[[Category: Double-stranded]] | |||
[[Category: Exodeoxyribonuclease v]] | |||
[[Category: Exodeoxyribonuclease]] | |||
[[Category: Helicase-nuclease]] | |||
[[Category: Homologous recombination]] | |||
[[Category: Hydrolase-dna complex]] | |||
Revision as of 16:55, 12 March 2014
Crystal structure of AddAB with a forked DNA substrateCrystal structure of AddAB with a forked DNA substrate
FunctionFunction
[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 StructureAbout this Structure
4ceh is a 3 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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