1beg

<StructureSection load='1beg' size='340' side='right'caption='[[1beg]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1beg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1beg OCA], [https://pdbe.org/1beg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1beg RCSB], [https://www.ebi.ac.uk/pdbsum/1beg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1beg ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/ELIB_PHYCR ELIB_PHYCR]] Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane.

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== Publication Abstract from PubMed ==

Cryptogein belongs to a new family of 10-kDa proteins called elicitins. Elicitins are necrotic and signaling proteins secreted by Phytophthora spp. responsible for the incompatible reaction and systemic hypersensitive-like necroses of diverse plant species leading to resistance against fungal or bacterial plant pathogens. The solution structure of beta cryptogein from Phytophthora cryptogea fungus was determined by using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. A set of 18 structures was calculated using 1360 NOE-derived distance restraints and 40 dihedral angle restraints obtained from 3JHNH alpha couplings. The RMS deviation from the mean structure is 0.87 +/- 0.14 A for backbone atoms and 1.34 +/- 0.14 A for all the non-hydrogen atoms of residues 2 to 98. The structure of beta cryptogein reveals a novel protein fold, with five helices and a double-stranded beta-sheet facing an omega-loop. One edge of the beta-sheet and the adjacent face of the omega-loop form a hydrophobic cavity. This cavity made of highly conserved residues represents a plausible binding site. Residue 13, which has been identified from directed mutagenesis and natural sequence comparison studies as a key amino acid involved in the differential control of necrosis, is surface exposed and could contribute to the binding to a ligand or a receptor. The solution structure is close to the X-ray structure, with slight differences lightly due to the crystal packing.

Three-dimensional solution structure of beta cryptogein, a beta elicitin secreted by a phytopathogenic fungus Phytophthora cryptogea.,Fefeu S, Bouaziz S, Huet JC, Pernollet JC, Guittet E Protein Sci. 1997 Nov;6(11):2279-84. PMID:9385630<ref>PMID:9385630</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bouaziz, S]]

[[Category: Fefeu, S]]

[[Category: Guittet, E]]

[[Category: Huet, J C]]

[[Category: Pernollet, J C]]

[[Category: Signalling protein]]