6QVA
Crystal structure of a CHAD domain from Chlorobium tepidum in complex with inorganic polyphosphate
6QVA の概要
| エントリーDOI | 10.2210/pdb6qva/pdb |
| 分子名称 | CHAD domain, 1,2-ETHANEDIOL, bis[oxidanyl-[oxidanyl-[oxidanyl(phosphonooxy)phosphoryl]oxy-phosphoryl]oxy-phosphoryl] hydrogen phosphate, ... (6 entities in total) |
| 機能のキーワード | four-helix bundle, inorganic polyphosphate binding protein, all alpha-helical protein, nuclear protein |
| 由来する生物種 | Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37588.40 |
| 構造登録者 | |
| 主引用文献 | Lorenzo-Orts, L.,Hohmann, U.,Zhu, J.,Hothorn, M. Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules. Life Sci Alliance, 2:-, 2019 Cited by PubMed Abstract: Inorganic polyphosphates (polyPs) are linear polymers of orthophosphate units linked by phosphoanhydride bonds. Here, we report that bacterial, archaeal, and eukaryotic conserved histidine α-helical (CHAD) domains are specific polyP-binding modules. Crystal structures reveal that CHAD domains are formed by two four-helix bundles, giving rise to a central pore surrounded by conserved basic surface patches. Different CHAD domains bind polyPs with dissociation constants ranging from the nano- to mid-micromolar range, but not nucleic acids. A CHAD-polyP complex structure reveals the phosphate polymer binding across the central pore and along the two basic patches. Mutational analysis of CHAD-polyP interface residues validates the complex structure. The presence of a CHAD domain in the polyPase ygiF enhances its enzymatic activity. The only known CHAD protein from the plant localizes to the nucleus/nucleolus when expressed in Arabidopsis and tobacco, suggesting that plants may harbor polyPs in these compartments. We propose that CHAD domains may be used to engineer the properties of polyP-metabolizing enzymes and to specifically localize polyP stores in eukaryotic cells and tissues. PubMed: 31133615DOI: 10.26508/lsa.201900385 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.05 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






