1yjo: Difference between revisions
New page: left|200px<br /><applet load="1yjo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjo, resolution 1.30Å" /> '''Structure of NNQQNY ... |
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[[Image:1yjo.gif|left|200px]]<br /><applet load="1yjo" size=" | [[Image:1yjo.gif|left|200px]]<br /><applet load="1yjo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1yjo, resolution 1.30Å" /> | caption="1yjo, resolution 1.30Å" /> | ||
'''Structure of NNQQNY from yeast prion Sup35 with zinc acetate'''<br /> | '''Structure of NNQQNY from yeast prion Sup35 with zinc acetate'''<br /> | ||
==Overview== | ==Overview== | ||
Numerous soluble proteins convert to insoluble amyloid-like fibrils that | 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== | ==About this Structure== | ||
1YJO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1YJO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Grothe, R.]] | [[Category: Grothe, R.]] | ||
[[Category: Madsen, A | [[Category: Madsen, A O.]] | ||
[[Category: Nelson, R.]] | [[Category: Nelson, R.]] | ||
[[Category: Riekel, C.]] | [[Category: Riekel, C.]] | ||
[[Category: Sawaya, M | [[Category: Sawaya, M R.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: steric zipper]] | [[Category: steric zipper]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:06 2008'' | ||
Revision as of 14:06, 21 February 2008
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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] with ZN and ACY as ligands. 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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