1a8l
From Proteopedia
(New page: 200px<br /><applet load="1a8l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a8l, resolution 1.90Å" /> '''PROTEIN DISULFIDE OX...) |
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| - | [[Image:1a8l.gif|left|200px]]<br /><applet load="1a8l" size=" | + | [[Image:1a8l.gif|left|200px]]<br /><applet load="1a8l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a8l, resolution 1.90Å" /> | caption="1a8l, resolution 1.90Å" /> | ||
'''PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS'''<br /> | '''PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein disulfide bond formation is a rate limiting step in protein | + | Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzymes belonging to the protein disulfide oxidoreductase superfamily, including protein disulfide isomerase (PDI) in eucarya and DsbA in bacteria. The first high resolution X-ray crystal structure of a protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus reveals structural details that suggest a relation to eukaryotic PDI. The protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif. The accessibilities of both active sites are rather different as are, very likely, their redox properties. The protein shows the ability to catalyze the oxidation of dithiols as well as the reduction of disulfide bridges. |
==About this Structure== | ==About this Structure== | ||
| - | 1A8L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1A8L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:03 2008'' |
Revision as of 09:42, 21 February 2008
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PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS
Overview
Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzymes belonging to the protein disulfide oxidoreductase superfamily, including protein disulfide isomerase (PDI) in eucarya and DsbA in bacteria. The first high resolution X-ray crystal structure of a protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus reveals structural details that suggest a relation to eukaryotic PDI. The protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif. The accessibilities of both active sites are rather different as are, very likely, their redox properties. The protein shows the ability to catalyze the oxidation of dithiols as well as the reduction of disulfide bridges.
About this Structure
1A8L is a Single protein structure of sequence from Pyrococcus furiosus with as ligand. Full crystallographic information is available from OCA.
Reference
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units., Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S, Ladenstein R, Nat Struct Biol. 1998 Jul;5(7):602-11. PMID:9665175
Page seeded by OCA on Thu Feb 21 11:42:03 2008
