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| {{STRUCTURE_1s8e| PDB=1s8e | SCENE= }} | | {{STRUCTURE_1s8e| PDB=1s8e | SCENE= }} |
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| '''Crystal structure of Mre11-3'''
| | ===Crystal structure of Mre11-3=== |
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| ==Overview==
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| The Mre11, Rad50 and Nbs1 proteins make up the conserved multi-functional Mre11 (MRN) complex involved in multiple, critical DNA metabolic processes including double-strand break repair and telomere maintenance. The Mre11 protein is a nuclease with broad substrate recognition, but MRN-dependent processes requiring the nuclease activity are not clearly defined. Here, we report the functional and structural characterization of a nuclease-deficient Mre11 protein termed mre11-3. Importantly, the hmre11-3 protein has wild-type ability to bind DNA, Rad50 and Nbs1; however, nuclease activity was completely abrogated. When expressed in cell lines from patients with ataxia telangiectasia-like disorder (ATLD), hmre11-3 restored the formation of ionizing radiation-induced foci. Consistent with the biochemical results, the 2.3 A crystal structure of mre11-3 from Pyrococcus furiosus revealed an active site structure with a wild-type-like metal-binding environment. The structural analysis of the H85L mutation provides a detailed molecular basis for the ability of mre11-3 to bind but not hydrolyze DNA. Together, these results establish that the mre11-3 protein provides an excellent system for dissecting nuclease-dependent and independent functions of the Mre11 complex. | | The line below this paragraph, {{ABSTRACT_PUBMED_15047855}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15047855 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15047855}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mre11]] | | [[Category: Mre11]] |
| [[Category: Rad50]] | | [[Category: Rad50]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:25:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:00:31 2008'' |
