8A1H
Bacterial 6-4 photolyase from Vibrio cholerase
Summary for 8A1H
| Entry DOI | 10.2210/pdb8a1h/pdb |
| Descriptor | 6-4 photolyase (FeS-BCP, CryPro), FLAVIN-ADENINE DINUCLEOTIDE, 1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol, ... (10 entities in total) |
| Functional Keywords | enzyme, iron-sulfur cluster, dna-repair, photoreceptor, dna binding protein |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 1 |
| Total formula weight | 65229.70 |
| Authors | Essen, L.-O.,Emmerich, H.J. (deposition date: 2022-06-01, release date: 2023-02-08, Last modification date: 2024-02-07) |
| Primary citation | Emmerich, H.J.,Schneider, L.,Essen, L.O. Structural and Functional Analysis of a Prokaryotic (6-4) Photolyase from the Aquatic Pathogen Vibrio Cholerae † . Photochem.Photobiol., 99:1248-1257, 2023 Cited by PubMed Abstract: Photolyases are flavoproteins, which are able to repair UV-induced DNA lesions in a light-dependent manner. According to their substrate, they can be distinguished as CPD- and (6-4) photolyases. While CPD-photolyases repair the predominantly occurring cyclobutane pyrimidine dimer lesion, (6-4) photolyases catalyze the repair of the less prominent (6-4) photoproduct. The subgroup of prokaryotic (6-4) photolyases/FeS-BCP is one of the most ancient types of flavoproteins in the ubiquitously occurring photolyase & cryptochrome superfamily (PCSf). In contrast to canonical photolyases, prokaryotic (6-4) photolyases possess a few particular characteristics, including a lumazine derivative as antenna chromophore besides the catalytically essential flavin adenine dinucleotide as well as an elongated linker region between the N-terminal α/β-domain and the C-terminal all-α-helical domain. Furthermore, they can harbor an additional short subdomain, located at the C-terminus, with a binding site for a [4Fe-4S] cluster. So far, two crystal structures of prokaryotic (6-4) photolyases have been reported. Within this study, we present the high-resolution structure of the prokaryotic (6-4) photolyase from Vibrio cholerae and its spectroscopic characterization in terms of in vitro photoreduction and DNA-repair activity. PubMed: 36692077DOI: 10.1111/php.13783 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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