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7YEC

TR-SFX MmCPDII-DNA complex: 6 ns snapshot. Includes 6 ns, dark, and extrapolated structure factors

Summary for 7YEC
Entry DOI10.2210/pdb7yec/pdb
Related7YC7 7YCM 7YCP 7YCR 7YD6 7YD7 7YD8 7YDZ 7YE0 7YEB
DescriptorDeoxyribodipyrimidine photolyase, CPD photolesion containing DNA, complementary oligonucleotide to the CPD containing DNA, ... (7 entities in total)
Functional Keywordsflavoprotein, photolyase, light driven electron transfer, dna repair, time-resolved serial crystallography., dna binding protein
Biological sourceMethanosarcina mazei
More
Total number of polymer chains6
Total formula weight129665.68
Authors
Primary citationMaestre-Reyna, M.,Wang, P.H.,Nango, E.,Hosokawa, Y.,Saft, M.,Furrer, A.,Yang, C.H.,Gusti Ngurah Putu, E.P.,Wu, W.J.,Emmerich, H.J.,Caramello, N.,Franz-Badur, S.,Yang, C.,Engilberge, S.,Wranik, M.,Glover, H.L.,Weinert, T.,Wu, H.Y.,Lee, C.C.,Huang, W.C.,Huang, K.F.,Chang, Y.K.,Liao, J.H.,Weng, J.H.,Gad, W.,Chang, C.W.,Pang, A.H.,Yang, K.C.,Lin, W.T.,Chang, Y.C.,Gashi, D.,Beale, E.,Ozerov, D.,Nass, K.,Knopp, G.,Johnson, P.J.M.,Cirelli, C.,Milne, C.,Bacellar, C.,Sugahara, M.,Owada, S.,Joti, Y.,Yamashita, A.,Tanaka, R.,Tanaka, T.,Luo, F.,Tono, K.,Zarzycka, W.,Muller, P.,Alahmad, M.A.,Bezold, F.,Fuchs, V.,Gnau, P.,Kiontke, S.,Korf, L.,Reithofer, V.,Rosner, C.J.,Seiler, E.M.,Watad, M.,Werel, L.,Spadaccini, R.,Yamamoto, J.,Iwata, S.,Zhong, D.,Standfuss, J.,Royant, A.,Bessho, Y.,Essen, L.O.,Tsai, M.D.
Visualizing the DNA repair process by a photolyase at atomic resolution.
Science, 382:eadd7795-eadd7795, 2023
Cited by
PubMed Abstract: Photolyases, a ubiquitous class of flavoproteins, use blue light to repair DNA photolesions. In this work, we determined the structural mechanism of the photolyase-catalyzed repair of a cyclobutane pyrimidine dimer (CPD) lesion using time-resolved serial femtosecond crystallography (TR-SFX). We obtained 18 snapshots that show time-dependent changes in four reaction loci. We used these results to create a movie that depicts the repair of CPD lesions in the picosecond-to-nanosecond range, followed by the recovery of the enzymatic moieties involved in catalysis, completing the formation of the fully reduced enzyme-product complex at 500 nanoseconds. Finally, back-flip intermediates of the thymine bases to reanneal the DNA were captured at 25 to 200 microseconds. Our data cover the complete molecular mechanism of a photolyase and, importantly, its chemistry and enzymatic catalysis at work across a wide timescale and at atomic resolution.
PubMed: 38033054
DOI: 10.1126/science.add7795
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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