2XRZ

X-ray structure of archaeal class II CPD photolyase from Methanosarcina mazei in complex with intact CPD-lesion

2XRZ の概要

• エントリーDOI: 10.2210/pdb2xrz/pdb
• 関連するPDBエントリー: 2XRY
• 分子名称: DEOXYRIBODIPYRIMIDINE PHOTOLYASE, CPD-COMPRISING OLIGONUCLEOTIDE, COUNTERSTRAND-OLIGONUCLEOTIDE, ... (8 entities in total)
• 機能のキーワード: lyase-dna complex, photolyase, dna damage, dna repair, class ii, intact cpd-lesion, protein-dna complex, water cluster, lyase/dna
• 由来する生物種: METHANOSARCINA MAZEI; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 130196.32

構造登録者

Kiontke, S.,Geisselbrecht, Y.,Pokorny, R.,Carell, T.,Batschauer, A.,Essen, L.O. (登録日: 2010-09-24, 公開日: 2011-09-14, 最終更新日: 2024-05-01)

主引用文献

Kiontke, S.,Geisselbrecht, Y.,Pokorny, R.,Carell, T.,Batschauer, A.,Essen, L.O.
Crystal Structures of an Archaeal Class II DNA Photolyase and its Complex with Uv-Damaged Duplex DNA.
Embo J., 30:4437-, 2011

PubMed Abstract: Class II photolyases ubiquitously occur in plants, animals, prokaryotes and some viruses. Like the distantly related microbial class I photolyases, these enzymes repair UV-induced cyclobutane pyrimidine dimer (CPD) lesions within duplex DNA using blue/near-UV light. Methanosarcina mazei Mm0852 is a class II photolyase of the archaeal order of Methanosarcinales, and is closely related to plant and metazoan counterparts. Mm0852 catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA. We solved crystal structures of Mm0852, the first one for a class II photolyase, alone and in complex with CPD lesion-containing duplex DNA. The lesion-binding mode differs from other photolyases by a larger DNA-binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophane dyad as electron transfer pathway to the catalytic FAD cofactor.

PubMed: 21892138
DOI: 10.1038/EMBOJ.2011.313

実験手法

X-RAY DIFFRACTION (2.2 Å)