2ma1

Solution structure of HRDC1 domain of RecQ helicase from Deinococcus radiodurans

spinqualitylabelsall models 2ma1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ma1 is a 1 chain structure with sequence from Deinococcus radiodurans R1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9RUU2_DEIRA Publication Abstract from PubMed The RecQ helicase from Deinococcus radiodurans (DrRecQ) distinguishes from other helicases in that it utilizes its three 'helicase and RNaseD C-terminal' domains (HRDC1, HRDC2 and HRDC3) to regulate its activity. These HRDC domains have different influence on the biochemical functions of DrRecQ. Currently, only the structure of HRDC3 was reported. Here, we determined the NMR structure of the N-terminal-most HRDC1, revealing a potential DNA binding domain. Fluorescence anisotropy assay indicates that HRDC1 has binding affinity weaker than 70 muM to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA. NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.,Liu S, Zhang W, Gao Z, Ming Q, Hou H, Lan W, Wu H, Cao C, Dong Y FEBS Lett. 2013 Aug 19;587(16):2635-42. doi: 10.1016/j.febslet.2013.06.048. Epub , 2013 Jul 4. PMID:23831579 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures

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