• Login
    Search 
    •   Home
    • Dept. Structure and function of proteins (SFPR)
    • Publications of the Dept. Structure and Functions of Proteins(SFPR)
    • Search
    •   Home
    • Dept. Structure and function of proteins (SFPR)
    • Publications of the Dept. Structure and Functions of Proteins(SFPR)
    • Search
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of HZICommunitiesTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)This CollectionTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)

    My Account

    LoginRegister

    Filter by Category

    JournalActa crystallographica. Section F, Structural biology communications (2)Current opinion in structural biology (1)Process Biochemistry (1)The Journal of biological chemistry (1)AuthorsBlankenfeldt, Wulf (2)Blankenfeldt, Wulf (2) ccKrausze, Joern (2)Berger, Ralf G. (1)Curth, Ute (1)View MoreYear (Issue Date)
    2014 (5)
    Types
    Article (5)

    Local Links

    About: PolicyHelmholtz-Zentrum für Infektionsforschung HomepageHZI-Library HomepageContact usOpen AccessPublishing ApproachGetting StartedEditing ProfileBrowsing OptionsUsing SearchSubmitting Content

    Statistics

    Display statistics
     

    Search

    Show Advanced FiltersHide Advanced Filters

    Filters

    Now showing items 1-5 of 5

    • List view
    • Grid view
    • Sort Options:
    • Relevance
    • Title Asc
    • Title Desc
    • Issue Date Asc
    • Issue Date Desc
    • Results Per Page:
    • 5
    • 10
    • 20
    • 40
    • 60
    • 80
    • 100

    • 5CSV
    • 5RefMan
    • 5EndNote
    • 5BibTex
    • Selective Export
    • Select All
    • Help
    Thumbnail

    Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.

    Hellert, Jan; Krausze, Joern; Schulz, Thomas F; Lührs, Thorsten (2014-11)
    The latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.
    Thumbnail

    Oligomerization inhibits Legionella pneumophila PlaB phospholipase A activity.

    Kuhle, Katja; Krausze, Joern; Curth, Ute; Rössle, Manfred; Heuner, Klaus; Lang, Christina; Flieger, Antje (2014-07-04)
    The intracellularly replicating lung pathogen Legionella pneumophila consists of an extraordinary variety of phospholipases, including at least 15 different phospholipases A (PLA). Among them, PlaB, the first characterized member of a novel lipase family, is a hemolytic virulence factor that exhibits the most prominent PLA activity in L. pneumophila. We analyzed here protein oligomerization, the importance of oligomerization for activity, addressed further essential regions for activity within the PlaB C terminus, and the significance of PlaB-derived lipolytic activity for L. pneumophila intracellular replication. We determined by means of analytical ultracentrifugation and small angle x-ray scattering analysis that PlaB forms homodimers and homotetramers. The C-terminal 5, 10, or 15 amino acids, although the individual regions contributed to PLA activity, were not essential for protein tetramerization. Infection of mouse macrophages with L. pneumophila wild type, plaB knock-out mutant, and plaB complementing or various mutated plaB-harboring strains showed that catalytic activity of PlaB promotes intracellular replication. We observed that PlaB was most active in the lower nanomolar concentration range but not at or only at a low level at concentration above 0.1 μm where it exists in a dimer/tetramer equilibrium. We therefore conclude that PlaB is a virulence factor that, on the one hand, assembles in inactive tetramers at micromolar concentrations. On the other hand, oligomer dissociation at nanomolar concentrations activates PLA activity. Our data highlight the first example of concentration-dependent phospholipase inactivation by tetramerization, which may protect the bacterium from internal PLA activity, but enzyme dissociation may allow its activation after export.
    Thumbnail

    Crystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD.

    Vit, Allegra; Misson, Laëtitia; Blankenfeldt, Wulf; Seebeck, Florian Peter (2014-05)
    Ergothioneine is an amino-acid betaine derivative of histidine that was discovered more than one century ago. Despite significant research pointing to a function in oxidative stress defence, the exact mechanisms of action of ergothioneine remain elusive. Although both humans and bacterial pathogens such as Mycobacterium tuberculosis seem to depend on ergothioneine, humans are devoid of the corresponding biosynthetic enzymes. Therefore, its biosynthesis may emerge as potential drug target in the development of novel therapeutics against tuberculosis. The recent identification of ergothioneine-biosynthetic genes in M. smegmatis enables a more systematic study of its biology. The pathway is initiated by EgtD, a SAM-dependent methyltransferase that catalyzes a trimethylation reaction of histidine to give N(α),N(α),N(α)-trimethylhistidine. Here, the recombinant production, purification and crystallization of EgtD are reported. Crystals of native EgtD diffracted to 2.35 Å resolution at a synchrotron beamline, whereas crystals of seleno-L-methionine-labelled protein diffracted to 1.75 Å resolution and produced a significant anomalous signal to 2.77 Å resolution at the K edge. All of the crystals belonged to space group P212121, with two EgtD monomers in the asymmetric unit.
    Thumbnail

    The structural biology of phenazine biosynthesis.

    Blankenfeldt, Wulf; Parsons, James F (2014-09-09)
    The phenazines are a class of over 150 nitrogen-containing aromatic compounds of bacterial and archeal origin. Their redox properties not only explain their activity as broad-specificity antibiotics and virulence factors but also enable them to function as respiratory pigments, thus extending their importance to the primary metabolism of phenazine-producing species. Despite their discovery in the mid-19th century, the molecular mechanisms behind their biosynthesis have only been unraveled in the last decade. Here, we review the contribution of structural biology that has led to our current understanding of phenazine biosynthesis.
    Thumbnail

    An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity

    Haase-Aschoff, Paul; Linke, Diana; Nimtz, Manfred; Popper, Lutz; Berger, Ralf G. (2014-01-14)
    DSpace software copyright © 2002-2019  DuraSpace
    Quick Guide | Kontakt | Feedback abschicken
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.