4aby

Crystal structure of Deinococcus radiodurans RecN head domain

spinqualitylabelsall models 4aby, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aby is a 4 chain structure with sequence from Deira. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 4abx Activity: Adenosinetriphosphatase, with EC number 3.6.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RECN_DEIRA] May be involved in recombinational repair of damaged DNA. Publication Abstract from PubMed Repair of DNA double-strand breaks (DSBs) is essential for cell survival and maintaining genome integrity. DSBs are repaired in a stepwise manner by homologous recombination. Here, we focused on the early steps of DSB repair, including DSB recognition, which is still only poorly understood. In prokaryotes, this process has been proposed to involve the RecN protein, a member of the structural maintenance of chromosome (SMC) protein family, which include key eukaryotic and prokaryotic proteins such as cohesin, condensin, and Rad50. An extensive high- and low-resolution structural analysis of Deinococcus radiodurans RecN using a combination of protein crystallography and small-angle X-ray scattering enabled us to assemble a quasi-atomic model of the entire RecN protein, representing the complete structure of a SMC-like protein. These results, together with a thorough biochemical and mutational study of RecN, allow us to propose a model for the role of RecN in DSB repair. Structural and Functional Characterization of an SMC-like Protein RecN: New Insights into Double-Strand Break Repair.,Pellegrino S, Radzimanowski J, de Sanctis D, Boeri Erba E, McSweeney S, Timmins J Structure. 2012 Dec 5;20(12):2076-89. doi: 10.1016/j.str.2012.09.010. Epub 2012, Oct 18. PMID:23085075 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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