2vim

X-ray structure of Fasciola hepatica thioredoxin

spinqualitylabelsall models 2vim, resolution 1.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vim is a 1 chain structure with sequence from Fasciola hepatica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.38Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9U1G7_FASHE Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Fasciola hepatica thioredoxin protein structure has been determined to 1.45A resolution. This is the first example of a single crystal structure to show the active site cysteine residues in both the reduced and disulfide oxidised form. Consistent with this observation the process of oxidation appears to require very little rearrangement of the surrounding protein structure. The F. hepatica thioredoxin structure has been compared to other thioredoxin protein structures already known and is found to be highly conserved. The F. hepatica protein is most similar to that of the thioredoxin from its human and animal hosts but it resembles other parasitic thioredoxins with regard to having no additional cysteine residues and is therefore not regulated by transient disulfide bond formation as proposed for thioredoxins from higher eukaryotic species. The Fasciola hepatica thioredoxin: High resolution structure reveals two oxidation states.,Line K, Isupov MN, Garcia-Rodriguez E, Maggioli G, Parra F, Littlechild JA Mol Biochem Parasitol. 2008 Sep;161(1):44-8. Epub 2008 Jun 21. PMID:18620002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Art:Thioredoxin: A small protein with a radical role Thioredoxin 3D structures

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