4nci

Crystal Structure of Pyrococcus furiosis Rad50 R805E mutationCrystal Structure of Pyrococcus furiosis Rad50 R805E mutation

FunctionFunction

[RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]

About this StructureAbout this Structure

4nci is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT. ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214 doi:http://dx.doi.org/10.1002/embj.201386100

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OCA

[1] Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT. ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling. EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214 doi:http://dx.doi.org/10.1002/embj.201386100

[xtra 1]