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File:Structure-and-Mechanism-of-Staphylococcus-aureus-TarS-the-Wall-Teichoic-Acid-β-glycosyltransferase-ppat.1006067.s009.ogv

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English: Structural morph among full-length TarS trimer monomers. TarS trimer monomers were overlayed along the trimerization domain, illustrating possible motion of relative catalytic domains. UDP-GlcNAc (blue) is displayed in stick form and colored according to heteroatom type.
Date
Source S1 Movie from Sobhanifar S, Worrall L, King D, Wasney G, Baumann L, Gale R, Nosella M, Brown E, Withers S, Strynadka N (2016). "Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance". PLOS Pathogens. DOI:10.1371/journal.ppat.1006067. PMID 27973583. PMC: 5156392.
Author Sobhanifar S, Worrall L, King D, Wasney G, Baumann L, Gale R, Nosella M, Brown E, Withers S, Strynadka N
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current23:57, 30 January 201724 s, 1,304 × 1,318 (6.05 MB)Open Access Media Importer Bot (talk | contribs)Automatically uploaded media file from Open Access source. Please report problems or suggestions here.

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