1tp9: Difference between revisions
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[[Image:1tp9.gif|left|200px]] | [[Image:1tp9.gif|left|200px]] | ||
'''PRX D (type II) from Populus tremula''' | {{Structure | ||
|PDB= 1tp9 |SIZE=350|CAPTION= <scene name='initialview01'>1tp9</scene>, resolution 1.62Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PRX D (type II) from Populus tremula''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TP9 is a [ | 1TP9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP9 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism., Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM, Biochemistry. 2005 Feb 15;44(6):1755-67. PMID:[http:// | Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism., Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM, Biochemistry. 2005 Feb 15;44(6):1755-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697201 15697201] | ||
[[Category: Populus trichocarpa]] | [[Category: Populus trichocarpa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
''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 14:21:25 2008'' | ||
Revision as of 15:21, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
PRX D (type II) from Populus tremula
OverviewOverview
Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.
About this StructureAbout this Structure
1TP9 is a Single protein structure of sequence from Populus trichocarpa. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism., Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM, Biochemistry. 2005 Feb 15;44(6):1755-67. PMID:15697201
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