3f4t

Crystal structure of Wolbachia pipientis alpha-DsbA1 C97A/C146A

spinqualitylabelsall models 3f4t, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3f4t is a 1 chain structure with sequence from Wolbachia endosymbiont of Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: 1PE, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q73GA4_WOLPM 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 alpha-Proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable development of inhibitors for chemical genetics studies. Wolbachia encodes a homolog (alpha-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia alpha-DsbA1 has the most reducing redox potential of any characterised DsbA. In addition, Wolbachia alpha-DsbA1 possesses a second disulfide that is highly conserved in alpha-Proteobacterial DsbAs but not in other DsbAs. The alpha-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of alpha-DsbA1 indicate that it probably plays a specialised oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies. STRUCTURAL AND FUNCTIONAL CHARACTERISATION OF THE OXIDOREDUCTASE alpha-DSBA1 FROM WOLBACHIA PIPIENTIS.,Kurz M, Iturbe-Ormaetxe I, Jarrott R, Shouldice SR, Wouters MA, Frei P, Glockshuber R, Oneill S, Heras B, Martin J Antioxid Redox Signal. 2009 Mar 5. PMID:19265485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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