Crystal structure of osmotin, a plant antifungal protein
نویسندگان
چکیده
منابع مشابه
Stress proteins on the yeast cell surface determine resistance to osmotin, a plant antifungal protein.
Strains of the yeast Saccharomyces cerevisiae differ in their sensitivities to tobacco osmotin, an antifungal protein of the PR-5 family. However, cells sensitive to tobacco osmotin showed resistance to osmotin-like proteins purified from the plant Atriplex nummularia, indicating a strict specificity between the antifungal protein and its target cell. A member of a gene family encoding stress p...
متن کاملCrystal structure of a nonsymbiotic plant hemoglobin.
BACKGROUND Nonsymbiotic hemoglobins (nsHbs) form a new class of plant proteins that is distinct genetically and structurally from leghemoglobins. They are found ubiquitously in plants and are expressed in low concentrations in a variety of tissues including roots and leaves. Their function involves a biochemical response to growth under limited O(2) conditions. RESULTS The first X-ray crystal...
متن کاملCharacterization of osmotin : a thaumatin-like protein associated with osmotic adaptation in plant cells.
Cultured tobacco (Nicotiana tabacum var Wisconsin 38) cells adapted to grow under osmotic stress synthesize and accumulate a 26 kilodalton protein (osmotin) which can constitute as much as 12% of total cellular protein. In cells adapted to NaCl, osmotin occurs in two forms: an aqueous soluble form (osmotin-I) and a detergent soluble form (osmotin II) in the approximate ratio of 2:3. Osmotin-I h...
متن کاملIn silico Analysis and Expression of Osmotin-EAAAK-LTP Fused Protein
Antifungal agents are causing different problems in the agriculture industry. Plants are using various defense mechanisms for resistance against fungal pathogens. Some examples of these mechanisms are making physical barriers, producing chemical components and pathogenesis-related proteins such as lipid transfer protein (LTP) and Osmotin which can inhibit the growth of fungi at micro-molar conc...
متن کاملCrystal structure of trbp111: a structure-specific tRNA-binding protein.
Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific tRNA-binding protein that has homologous counterparts distributed throughout evolution. A dimer is the functional unit for binding a single tRNA. Here we report the 3D structures of the A.aeolicus protein and its Escherichia coli homolog at resolutions of 2.50 and 1.87 A, respectively. The structure shows a symmetrical dimer of two...
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ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Bioinformatics
سال: 2003
ISSN: 0887-3585
DOI: 10.1002/prot.10571