2apq
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Crystal Structure of an Active Site Mutant of Bovine Pancreatic Ribonuclease A (H119A-RNase A) with a 10-Glutamine expansion in the C-terminal hinge-loop.
OverviewOverview
Amyloid or amyloid-like fibrils are elongated, insoluble protein, aggregates, formed in vivo in association with neurodegenerative diseases, or in vitro from soluble native proteins, respectively. The underlying, structure of the fibrillar or 'cross-beta' state has presented, long-standing, fundamental puzzles of protein structure. These include, whether fibril-forming proteins have two structurally distinct stable, states, native and fibrillar, and whether all or only part of the native, protein refolds as it converts to the fibrillar state. Here we show that a, designed amyloid-like fibril of the well-characterized enzyme RNase A, contains native-like molecules capable of enzymatic activity. In addition, these functional molecular units are formed from a core RNase A domain and, a swapped complementary domain. These findings are consistent with the, zipper-spine model in which a cross-beta spine is decorated with, three-dimensional domain-swapped functional units, retaining native-like, structure.
About this StructureAbout this Structure
2APQ is a Single protein structure of sequence from Bos taurus with PO4 as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
ReferenceReference
Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure., Sambashivan S, Liu Y, Sawaya MR, Gingery M, Eisenberg D, Nature. 2005 Sep 8;437(7056):266-9. PMID:16148936
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