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5ZC3

The Crystal Structure of PcRxLR12

Summary for 5ZC3
Entry DOI10.2210/pdb5zc3/pdb
DescriptorRxLR effector (1 entity in total)
Functional Keywordsrxlr effectors, immunosuppressant
Biological sourcePhytophthora capsici
Total number of polymer chains2
Total formula weight107110.16
Authors
Zhao, L.,Zhang, X.,Zhu, C. (deposition date: 2018-02-14, release date: 2018-08-15, Last modification date: 2024-10-30)
Primary citationZhao, 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: 30077372
DOI: 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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