2rnm | pdb_00002rnm

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Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

spinqualitylabelsall models 2rnm, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rnm is a 5 chain structure with sequence from Podas. The May 2008 RCSB PDB Molecule of the Month feature on Prions by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_5. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [HETS_PODAS] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function. Publication Abstract from PubMed Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the prion function. However, no atomic-resolution structure of the fibrillar state that is likely infectious has been reported to date. We present a structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina. On the basis of 134 intra- and intermolecular experimental distance restraints, we find that HET-s(218-289) forms a left-handed beta solenoid, with each molecule forming two helical windings, a compact hydrophobic core, at least 23 hydrogen bonds, three salt bridges, and two asparagine ladders. The structure is likely to have broad implications for understanding the infectious amyloid state. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.,Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH Science. 2008 Mar 14;319(5869):1523-6. PMID:18339938 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Prion Prion protein

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