2l0m

DsbB2 peptide structure in 100% TFE

spinqualitylabelsall models 2l0m, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l0m is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2zuq, 2k73 Resources: FirstGlance, OCA, RCSB, PDBsum Function [C4ZTM6_ECOBW] Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.[HAMAP-Rule:MF_00286] Publication Abstract from PubMed The two-stage model for membrane protein folding postulates that individual helices form first and are subsequently packed against each other. To probe the two-stage model, the structures of peptides representing individual transmembrane helices of the disulfide bond forming protein B have been studied in trifluoroethanol solution as well as in detergent micelles using nuclear magnetic resonance (NMR) and circular dichroism spectroscopy. In TFE solution, peptides showed well-defined alpha-helical structures. Peptide structures in TFE were compared to the structures of full-length protein obtained by X-ray crystallography and NMR. The extent of alpha-helical secondary structure coincided well, lending support for the two-stage model for membrane protein folding. However, the conformation of some amino acid side chains differs between the structures of peptide and full-length protein. In micellar solution, the peptides also adopted a helical structure, albeit of reduced definition. Using measurements of paramagnetic relaxation enhancement, peptides were confirmed to be embedded in micelles. These observations may indicate that in the native protein, tertiary interactions additionally stabilize the secondary structure of the individual transmembrane helices. Proteins 2011. (c) 2011 Wiley-Liss, Inc. Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy.,Hwang S, Hilty C Proteins. 2011 Jan 4. doi: 10.1002/prot.22877. PMID:21337621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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