http://hdl.handle.net/10033/6833 Wed, 22 May 2013 00:44:34 GMT 2013-05-22T00:44:34Z http://hdl.handle.net/10033/270795 Title: Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). Authors: Glotzbach, Bernhard; Schmelz, Stefan; Reinwarth, Michael; Christmann, Andreas; Heinz, Dirk W; Kolmar, Harald Abstract: In recent decades, several canonical serine protease inhibitor families have been classified and characterized. In contrast to most trypsin inhibitors, those from garden four o'clock (Mirabilis jalapa) and spinach (Spinacia oleracea) do not share sequence similarity and have been proposed to form the new Mirabilis serine protease inhibitor family. These 30-40-amino-acid inhibitors possess a defined disulfide-bridge topology and belong to the cystine-knot miniproteins (knottins). To date, no atomic structure of this inhibitor family has been solved. Here, the first structure of S. oleracea trypsin inhibitor III (SOTI-III), in complex with bovine pancreatic trypsin, is reported. The inhibitor was synthesized by solid-phase peptide synthesis on a multi-milligram scale and was assayed to test its inhibitory activity and binding properties. The structure confirmed the proposed cystine-bridge topology. The structural features of SOTI-III suggest that it belongs to a new canonical serine protease inhibitor family with promising properties for use in protein-engineering and medical applications. Tue, 01 Jan 2013 00:00:00 GMT http://hdl.handle.net/10033/270795 2013-01-01T00:00:00Z http://hdl.handle.net/10033/250993 Title: Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli. Authors: de Groot, Jens C; Schlüter, Kai; Carius, Yvonne; Quedenau, Claudia; Vingadassalom, Didier; Faix, Jan; Weiss, Stefanie M; Reichelt, Joachim; Standfuss-Gabisch, Christine; Lesser, Cammie F; Leong, John M; Heinz, Dirk W; Büssow, Konrad; Stradal, Theresia E B Abstract: Actin assembly beneath enterohemorrhagic E. coli (EHEC) attached to its host cell is triggered by the intracellular interaction of its translocated effector proteins Tir and EspF(U) with human IRSp53 family proteins and N-WASP. Here, we report the structure of the N-terminal I-BAR domain of IRSp53 in complex with a Tir-derived peptide, in which the homodimeric I-BAR domain binds two Tir molecules aligned in parallel. This arrangement provides a protein scaffold linking the bacterium to the host cell's actin polymerization machinery. The structure uncovers a specific peptide-binding site on the I-BAR surface, conserved between IRSp53 and IRTKS. The Tir Asn-Pro-Tyr (NPY) motif, essential for pedestal formation, is specifically recognized by this binding site. The site was confirmed by mutagenesis and in vivo-binding assays. It is possible that IRSp53 utilizes the NPY-binding site for additional interactions with as yet unknown partners within the host cell. Wed, 07 Sep 2011 00:00:00 GMT http://hdl.handle.net/10033/250993 2011-09-07T00:00:00Z http://hdl.handle.net/10033/245191 Title: Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx. Authors: Wilke, Sonja; Krausze, Joern; Büssow, Konrad Abstract: ABSTRACT: Sun, 01 Jan 2012 00:00:00 GMT http://hdl.handle.net/10033/245191 2012-01-01T00:00:00Z http://hdl.handle.net/10033/230947 Title: Biosynthesis of the repeating units of the exopolysaccharides amylovoran from Erwinia amylovora and stewartan from Pantoea stewartii Authors: Langlotz, Christine; Schollmeyer, Martin; Coplin, David L.; Nimtz, Manfred; Geider, Klaus Wed, 27 Jun 2012 00:00:00 GMT http://hdl.handle.net/10033/230947 2012-06-27T00:00:00Z