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These domains are necessary for accurate cell wall recognition 81314 and have been shown to recognize and bind glycine cross-bridges characteristic for most staphylococci Twitter may be over capacity or experiencing a momentary hiccup. The error bars represent standard deviation calculated for three experiments each run with triplicates. Close Create a new list. Don't have an account?

  • Structural bases of peptidoglycan recognition by lysostaphin SH3b domain Scientific Reports
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  • Izabela Stefaniak | Read 4 publications, and contact Izabela Stefaniak on the quality of the avatar's speech and its synchronization with the animations.

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    View. Izabela Stefaniak at Institute of Psychiatry and Neurology, Warsaw, Poland.

    Structural bases of peptidoglycan recognition by lysostaphin SH3b domain Scientific Reports

    Izabela Stefaniak. Institute of Psychiatry and Neurology, Warsaw.

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    Endolysins as antimicrobials. Izabela Stefaniak. We have solved the crystal structure of the lysostaphin SH3b domain in complex with a pentaglycine peptide representing the peptidoglycan cross-bridge.

    Zoll, S. To explore further the conformational space of the PG fragment upon interaction with the SH3b domain, we performed MD analyses at higher temperatures Fig.

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    J Biosci Bioeng55—61 Yu, W.

    This is consistent with the observation that a change from glycine to serine in the peptidoglycan of lysostaphin-resistant staphylococci protects against lysostaphin activity and diminishes binding to the SH3b domain 14 The only variations are found in loop regions, mainly distal and extra loops.

    This mutagenesis was performed both on LssSH3b fused to GFP to characterize binding properties and on mature lysostaphin to test their effect on lytic activity of the enzyme.

    PavlovAnna S. A Structure of ligand PG fragment used for modeling.

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    Izabela Stefaniak, Kamil Sorokosz, Artur Janicki, Jacek Wciórka. .

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    The K d was determined by nonlinear fitting of the thermophoresis responses using the NTAnalysis software.

    Neese, F. Moreover, the Gly3 replacement by serine iv allows for intramolecular hydrogen bond interactions between the hydroxymethyl side chain and the main chain of the ligand.

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    Figure 8. The Gly3 NH group points towards solvent and hydrogen bonds to a water molecule.

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    BokshaNikita B. Substrate selectivity versus binding affinity The main concern related to application of lysostaphin as an antimicrobial is resistance, which already exists in nature.

    Although structures of SH3bs from lysostaphin are available, the binding modes of peptidoglycan to these domains are still unclear.

    Tossavainen, H. Loessner, M. These domains are necessary for accurate cell wall recognition 81314 and have been shown to recognize and bind glycine cross-bridges characteristic for most staphylococci Open Babel: An open chemical toolbox.

    5 Replies to “Izabela stefaniak animated”

    1. Similarly to our observations, substitution of the asparagine in SH3b domain from LysGH15 lysine corresponding to N in lysostaphin SH3b domain had a significant effect on peptidoglycan binding which was much less pronounced in the lytic activity assays

    2. We and our partners operate globally and use cookies, including for analytics, personalisation, and ads. Bioinformatic tools helped to analyze the consequences of substituting the middle glycine with serine, which is known mechanism of SH3b binding inhibition

    3. B Alignment of amino acid sequence of SH3b domains from lysostaphin and Ale On the contrary, the cross-linked stem peptide can adopt different conformations interacting via hydrogen bonds with different parts of SH3b surface.