6LCM
Crystal structure of chloroplast resolvase ZmMOC1 with the magic triangle I3C
Summary for 6LCM
| Entry DOI | 10.2210/pdb6lcm/pdb |
| Descriptor | ZmMoc1, 5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid (3 entities in total) |
| Functional Keywords | chloroplast, resolvase, holliday junction, plant protein, hydrolase |
| Biological source | Zea mays (Maize) |
| Total number of polymer chains | 1 |
| Total formula weight | 20759.27 |
| Authors | Yan, J.J.,Hong, S.X.,Guan, Z.Y.,Yin, P. (deposition date: 2019-11-19, release date: 2020-04-08, Last modification date: 2024-03-27) |
| Primary citation | Yan, J.,Hong, S.,Guan, Z.,He, W.,Zhang, D.,Yin, P. Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1. Nat Commun, 11:1417-1417, 2020 Cited by PubMed Abstract: Holliday junctions (HJs) are key DNA intermediates in genetic recombination and are eliminated by nuclease, termed resolvase, to ensure genome stability. HJ resolvases have been identified across all kingdoms of life, members of which exhibit sequence-dependent HJ resolution. However, the molecular basis of sequence selectivity remains largely unknown. Here, we present the chloroplast resolvase MOC1, which cleaves HJ in a cytosine-dependent manner. We determine the crystal structure of MOC1 with and without HJs. MOC1 exhibits an RNase H fold, belonging to the retroviral integrase family. MOC1 functions as a dimer, and the HJ is embedded into the basic cleft of the dimeric enzyme. We characterize a base recognition loop (BR loop) that protrudes into and opens the junction. Residues from the BR loop intercalate into the bases, disrupt the C-G base pairing at the crossover and recognize the cytosine, providing the molecular basis for sequence-dependent HJ resolution by a resolvase. PubMed: 32184398DOI: 10.1038/s41467-020-15242-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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