1yjo
From Proteopedia
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| - | [[Image:1yjo.gif|left|200px]] | + | [[Image:1yjo.gif|left|200px]] |
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| - | '''Structure of NNQQNY from yeast prion Sup35 with zinc acetate''' | + | {{Structure |
| + | |PDB= 1yjo |SIZE=350|CAPTION= <scene name='initialview01'>1yjo</scene>, resolution 1.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of NNQQNY from yeast prion Sup35 with zinc acetate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YJO is a [ | + | 1YJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJO OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the cross-beta spine of amyloid-like fibrils., Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D, Nature. 2005 Jun 9;435(7043):773-8. PMID:[http:// | + | Structure of the cross-beta spine of amyloid-like fibrils., Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D, Nature. 2005 Jun 9;435(7043):773-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15944695 15944695] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Balbirnie, M.]] | [[Category: Balbirnie, M.]] | ||
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[[Category: steric zipper]] | [[Category: steric zipper]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:45 2008'' |
Revision as of 13:23, 20 March 2008
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| , resolution 1.30Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of NNQQNY from yeast prion Sup35 with zinc acetate
Overview
Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.
About this Structure
1YJO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of the cross-beta spine of amyloid-like fibrils., Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D, Nature. 2005 Jun 9;435(7043):773-8. PMID:15944695
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