5ZC3
The Crystal Structure of PcRxLR12
Summary for 5ZC3
| Entry DOI | 10.2210/pdb5zc3/pdb |
| Descriptor | RxLR effector (1 entity in total) |
| Functional Keywords | rxlr effectors, immunosuppressant |
| Biological source | Phytophthora capsici |
| Total number of polymer chains | 2 |
| Total formula weight | 107110.16 |
| Authors | |
| Primary citation | Zhao, L.,Zhang, X.,Zhang, X.,Song, W.,Li, X.,Feng, R.,Yang, C.,Huang, Z.,Zhu, C. Crystal structure of the RxLR effector PcRxLR12 from Phytophthora capsici Biochem. Biophys. Res. Commun., 503:1830-1835, 2018 Cited by PubMed Abstract: RxLR genes are a prominent class of effectors in oomycetes, and almost half of these proteins contain a conserved sequence motif termed the WY domain, that may exist singly, or as divergent tandem repeats in different effectors. Here we describe the crystal structure of PcRxLR12 (63-488) from Phytophthora capsici at 3.0 Å resolution. The structure consists of five tandemly arrayed WY-domains linked to each other by short connecting helices. Superposition of the WY-2 domain on the other four domains of PcRxLR12, show that the first α-helix termed the K motif, and Loop 3 which connects α and α are the key regions of structural divergence between the WY domains. A similar pattern was observed when WY-2 was superposed on the 11 WY domains from other oomycete effectors. We also note that an added connecting helix between WY domains in some RXLR effectors, ensures that the WY domains are oriented in the same direction. PubMed: 30077372DOI: 10.1016/j.bbrc.2018.07.121 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.005 Å) |
Structure validation
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