2apq
From Proteopedia
(New page: 200px<br /><applet load="2apq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2apq, resolution 1.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:2apq.gif|left|200px]]<br /><applet load="2apq" size=" | + | [[Image:2apq.gif|left|200px]]<br /><applet load="2apq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2apq, resolution 1.80Å" /> | caption="2apq, resolution 1.80Å" /> | ||
'''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.'''<br /> | '''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.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Amyloid or amyloid-like fibrils are elongated, insoluble protein | + | 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 Structure== | ==About this Structure== | ||
| - | 2APQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http:// | + | 2APQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2APQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: Sambashivan, S.]] | [[Category: Sambashivan, S.]] | ||
| - | [[Category: Sawaya, M | + | [[Category: Sawaya, M R.]] |
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: an active site mutant of rnase a (h119a) with an amyloidogenic expansion in the c-terminal hinge-loop region(between residues 112 and 113).]] | [[Category: an active site mutant of rnase a (h119a) with an amyloidogenic expansion in the c-terminal hinge-loop region(between residues 112 and 113).]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:29:41 2008'' |
Revision as of 14:29, 21 February 2008
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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.
Overview
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 Structure
2APQ is a Single protein structure of sequence from Bos taurus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
Reference
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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