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  • Ficner, Ralf  (4)
  • Chemistry
Type of Medium
  • 1
    Language: English
    In: Current Opinion in Structural Biology, 2011, Vol.21(2), pp.232-239
    Description: Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.
    Keywords: Biology ; Chemistry
    ISSN: 0959-440X
    E-ISSN: 1879-033X
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  • 2
    Language: English
    In: BBA - Molecular Cell Research, August 2015, Vol.1853(8), pp.1850-1859
    Description: The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (AAC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor.
    Keywords: Tom70 ; Mitochondria ; Protein Import ; Presequence ; Biology ; Chemistry
    ISSN: 0167-4889
    E-ISSN: 1879-2596
    E-ISSN: 18782434
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  • 3
    Language: English
    In: Journal of Molecular Biology, 2010, Vol.397(1), pp.341-351
    Description: An α-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as K1 and and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia molecule is bound in an extended conformation representing the enzyme–product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.
    Keywords: Polysialic Acid ; Endonf ; Glycosidase ; Host Recognition ; Biology ; Chemistry
    ISSN: 0022-2836
    E-ISSN: 1089-8638
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  • 4
    In: Acta Crystallographica Section D, 01 February 2010, Vol.66(2), pp.176-180
    Description: Endosialidase NF (endoNF) is a bacteriophage‐derived endosialidase that specifically degrades α‐2,8‐linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 Å resolution. The 210 kDa homotrimeric multi‐domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active‐site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.
    Keywords: Endosialidase Nf ; Polysialic Acid ; Atomic Resolution
    ISSN: 0907-4449
    E-ISSN: 1399-0047
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