1tp9: Difference between revisions

Revision as of 13:02, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tp9.png

Template:STRUCTURE 1tp9

PRX D (type II) from Populus tremulaPRX D (type II) from Populus tremula

Template:ABSTRACT PUBMED 15697201

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

Page seeded by OCA on Mon Jul 28 13:02:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''PRX D (type II) from Populus tremula'''
+===PRX D (type II) from Populus tremula===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15697201}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15697201 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15697201}}
 ==About this Structure==
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 [[Category: Peroxiredoxin]]
 [[Category: Thioredoxin fold]]
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