Crystal structure of the RxLR effector PcRxLR12 from Phytophthora capsici

Biochem Biophys Res Commun. 2018 Sep 10;503(3):1830-1835. doi: 10.1016/j.bbrc.2018.07.121. Epub 2018 Aug 1.

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 α3 and α4 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.

Keywords: Crystal structure; Oomycete; Pathogen; Virulence factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Fungal Proteins / chemistry*
  • Models, Molecular
  • Phytophthora / chemistry*
  • Protein Conformation

Substances

  • Fungal Proteins