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NMR solution structure of a cyanovirin homolog from wheat head blight fungus
Author(s) -
Matei Elena,
Louis John M.,
Jee JunGoo,
Gronenborn Angela M.
Publication year - 2011
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22981
Subject(s) - fungus , head (geology) , blight , biology , botany , paleontology
Members of the cyanovirin‐N homolog (CVNH) lectin family are found in bacteria, fungi and plants. As part of our ongoing work on CVNH structure‐function studies, we determined the high‐resolution NMR solution structure of the homolog from the wheat head blight disease causing ascomycetous fungus Gibberella zeae (or Fusarium graminearum ), hereafter called GzCVNH. Like cyanovirin‐N (CV‐N), GzCVNH comprises two tandem sequence repeats and the protein sequence exhibits 30% identity with CV‐N. The overall structure is similar to those of other members of the CVNH family, with the conserved pseudo‐symmetric halves of the structure, domains A and B, closely resembling recently determined structures of Tuber borchii , Neurospora crassa, and Ceratopteris richardii CVNH proteins. Although GzCVNH exhibits a similar glycan recognition profile to CV‐N and specifically binds to Manα(1‐2)Manα, its weak carbohydrate binding affinity to only one binding site is insufficient for conferring anti‐HIV activity. Proteins 2011; © 2011 Wiley‐Liss, Inc.