6QV5
Crystal structure of the CHAD domain from the plant Ricinus communis
Summary for 6QV5
| Entry DOI | 10.2210/pdb6qv5/pdb |
| Descriptor | CHAD domain, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | four-helix bundle, inorganic polyphosphate binding protein, all alpha-helical protein, nuclear protein |
| Biological source | Ricinus communis (Castor bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 33341.67 |
| Authors | Lorenzo-Orts, L.,Hothorn, M. (deposition date: 2019-03-01, release date: 2019-05-29, Last modification date: 2024-05-15) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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