1yjo
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1yjo |SIZE=350|CAPTION= <scene name='initialview01'>1yjo</scene>, resolution 1.30Å | |PDB= 1yjo |SIZE=350|CAPTION= <scene name='initialview01'>1yjo</scene>, resolution 1.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yjp|1YJP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjo OCA], [http://www.ebi.ac.uk/pdbsum/1yjo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yjo RCSB]</span> | ||
}} | }} | ||
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[[Category: Riekel, C.]] | [[Category: Riekel, C.]] | ||
[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: ZN]] | ||
[[Category: asparagine zipper]] | [[Category: asparagine zipper]] | ||
[[Category: glutamine zipper]] | [[Category: glutamine zipper]] | ||
| Line 35: | Line 36: | ||
[[Category: steric zipper]] | [[Category: steric zipper]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:09:55 2008'' |
Revision as of 22:09, 30 March 2008
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| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1YJP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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