8A1H

Bacterial 6-4 photolyase from Vibrio cholerase

8A1H の概要

• エントリーDOI: 10.2210/pdb8a1h/pdb
• 分子名称: 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)
• 機能のキーワード: enzyme, iron-sulfur cluster, dna-repair, photoreceptor, dna binding protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65229.70

構造登録者

Essen, L.-O.,Emmerich, H.J. (登録日: 2022-06-01, 公開日: 2023-02-08, 最終更新日: 2024-02-07)

主引用文献

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

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: 36692077
DOI: 10.1111/php.13783

実験手法

X-RAY DIFFRACTION (1.65 Å)