6J44
Crystal structure of the redefined DNA-binding domain of human XPA
Summary for 6J44
| Entry DOI | 10.2210/pdb6j44/pdb |
| Descriptor | DNA repair protein complementing XP-A cells, ZINC ION (3 entities in total) |
| Functional Keywords | dna repair, nucleotide excision repair, scaffold protein, zinc finger, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 17538.58 |
| Authors | Lian, F.M.,Yang, X.,Yang, W.,Jiang, Y.L.,Qian, C. (deposition date: 2019-01-07, release date: 2019-05-29, Last modification date: 2024-03-27) |
| Primary citation | Lian, F.M.,Yang, X.,Yang, W.,Jiang, Y.L.,Qian, C. Structural characterization of the redefined DNA-binding domain of human XPA. Biochem.Biophys.Res.Commun., 514:985-990, 2019 Cited by PubMed Abstract: XPA (xeroderma pigmentosum complementation group A), a key scaffold protein in nucleotide excision repair (NER) pathway, is important in DNA damage verification and repair proteins recruitment. Earlier studies had mapped the minimal DNA-binding domain (MBD) of XPA to a region corresponding to residues 98-219. However, recent studies indicated that the region involving residues 98-239 is the redefined DNA-binding domain (DBD), which binds to DNA substrates with a much higher binding affinity than MBD and possesses a nearly identical binding affinity to the full-length XPA protein. However, the structure of the redefined DBD domain of XPA (XPA-DBD) remains to be investigated. Here, we present the crystal structure of XPA-DBD at 2.06 Å resolution. Structure of the C-terminal region of XPA has been extended by 21 residues (Arg211-Arg231) as compared with previously reported MBD structures. The structure reveals that the C-terminal extension (Arg211-Arg231) is folded as an α-helix with multiple basic residues. The positively charged surface formed in the last C-terminal helix suggests its critical role in DNA binding. Further structural analysis demonstrates that the last C-terminal region (Asp217-Thr239) of XPA-DBD might undergo a conformational change to directly bind to the DNA substrates. This study provides a structural basis for understanding the possible mechanism of enhanced DNA-binding affinity of XPA-DBD. PubMed: 31092331DOI: 10.1016/j.bbrc.2019.05.050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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