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The structure of Plasmodium falciparum 3D7_0606800 reveals a bi‐lobed architecture that supports re‐annotation as a Venus Flytrap protein
Author(s) -
Parker Michelle L.,
Ramaswamy Raghavendran,
van Gordon Kyle,
Powell Cameron J.,
Bosch Jürgen,
Boulanger Martin J.
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3218
Subject(s) - plasmodium falciparum , venus , computational biology , biology , botany , microbiology and biotechnology , physics , chemistry , astrobiology , malaria , immunology
Plasmodium falciparum , the causative agent of malaria, employs a diverse array of surface displayed proteins to promote dissemination and establish infection in the human host. Of these, Pf3D7_0606800 is highly immunogenic and has been designated a potential top 10 candidate for inclusion in a multicomponent malarial vaccine. The role of Pf3D7_0606800 in parasite biology, however, is unknown and its characterization has been complicated by a lack of sequence identity with proteins of known structure or function. Towards elucidating Pf3D7_0606800 function, we determined its structure to a resolution of 2.35 Å using selenium single wavelength anomalous dispersion. A bi‐lobed architecture displays the core structural hallmarks of V enus F ly t rap (VFT) proteins prompting us to re‐annotate Pf3D7_0606800 as PfVFT1. Structural analysis further revealed an extended inter‐lobe groove that, when interrogated by molecular docking, appears well suited to bind peptide‐based ligands. Collectively, our structural characterization of the highly antigenic P. falciparum surface protein PfVFT1 provides intriguing functional insight and establishes a structural template that could prove valuable for malaria vaccine engineering studies.