8YVA
Crystal structure of Caenorhabditis elegans ZIM-2 ZF1-2-CTD domain in complex with Chromosome V pairing center
Summary for 8YVA
Entry DOI | 10.2210/pdb8yva/pdb |
Descriptor | C2H2-type domain-containing protein, DNA (5'-D(*TP*TP*GP*GP*GP*CP*GP*CP*TP*GP*CP*T)-3'), DNA (5'-D(*AP*GP*CP*AP*GP*CP*GP*CP*CP*CP*AP*A)-3'), ... (5 entities in total) |
Functional Keywords | doule stranded dna binding protein, dna binding protein |
Biological source | Caenorhabditis elegans More |
Total number of polymer chains | 6 |
Total formula weight | 44503.60 |
Authors | |
Primary citation | Li, M.,Zhu, C.,Xu, Z.,Xu, M.,Kuang, Y.,Hou, X.,Huang, X.,Lv, M.,Liu, Y.,Zhang, Y.,Xu, Z.,Han, X.,Wang, S.,Shi, Y.,Guang, S.,Li, F. Structural basis for C. elegans pairing center DNA binding specificity by the ZIM/HIM-8 family proteins. Nat Commun, 15:10355-10355, 2024 Cited by PubMed Abstract: Pairing center (PC) on each chromosome of Caenorhabditis elegans is crucial for homolog pairing and initiating synapsis. Within each PC, clusters of 11/12 bp DNA motif recruit one of four paralogous meiosis-specific proteins: ZIM-1, ZIM-2, ZIM-3, or HIM-8. However, the mechanistic basis underlying the specificity of ZIM/HIM-8-PC DNA interaction remains elusive. Here, we describe crystal structures of HIM-8, ZIM-1 and ZIM-2 DNA binding domains (ZF1, ZF2 and CTD) in complex with their cognate PC DNA motifs, respectively. These structures demonstrated the ZF1-2-CTD folds as an integrated structural unit crucial for its DNA binding specificity. Base-specific DNA-contacting residues are exclusively distributed on ZF1-2 and highly conserved. Furthermore, the CTD potentially contributes to the conformational diversity of ZF1-2, imparting binding specificity to distinct PC DNA motifs. These findings shed light on the mechanism governing PC DNA motif recognition by ZIM/HIM-8 proteins, suggesting a co-evolution relationship between PC DNA motifs and ZF1-2-CTD in shaping the specific recognition. PubMed: 39609407DOI: 10.1038/s41467-024-54548-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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