2q2e | pdb_00002q2e

Crystal structure of the topoisomerase VI holoenzyme from Methanosarcina mazei

spinqualitylabelsall models 2q2e, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2q2e is a 2 chain structure with sequence from Dsm 2053. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: top6A (DSM 2053), top6B (DSM 2053) Activity: DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TOP6A_METMA] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00132] [TOP6B_METMA] Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity).[HAMAP-Rule:MF_00322] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Type II topoisomerases help disentangle chromosomes to facilitate cell division. To advance understanding of the structure and dynamics of these essential enzymes, we have determined the crystal structure of an archaeal type IIB topoisomerase, topo VI, at 4.0-A resolution. The 220-kDa heterotetramer adopts a 'twin-gate' architecture, in which a pair of ATPase domains at one end of the enzyme is poised to coordinate DNA movements into the enzyme and through a set of DNA-cleaving domains at the other end. Small-angle X-ray scattering studies show that nucleotide binding elicits a major structural reorganization that is propagated to the enzyme's DNA-cleavage center, explaining how ATP is coupled to DNA capture and strand scission. These data afford important insights into the mechanisms of topo VI and related proteins, including type IIA topoisomerases and the Spo11 meiotic recombination endonuclease. Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI.,Corbett KD, Benedetti P, Berger JM Nat Struct Mol Biol. 2007 Jul;14(7):611-9. Epub 2007 Jul 1. PMID:17603498 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Topoisomerase 3D structures WD-repeat protein 3D structures

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