3ny6

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Template:STRUCTURE 3ny6

Contents

Catalytic fragment of cholix toxin from vibrio cholerae in complex with inhibitor V30

Template:ABSTRACT PUBMED 21135177

Function

[Q5EK40_VIBCH] An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.[1] [2]

About this Structure

3ny6 is a 1 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA.

Reference

  • Turgeon Z, Jorgensen R, Visschedyk D, Edwards PR, Legree S, McGregor C, Fieldhouse RJ, Mangroo D, Schapira M, Merrill AR. Newly Discovered and Characterized Antivirulence Compounds inhibit Bacterial Mono-ADP-ribosyltransferase Toxins. Antimicrob Agents Chemother. 2010 Dec 6. PMID:21135177 doi:10.1128/AAC.01164-10
  1. ↑ Jorgensen R, Purdy AE, Fieldhouse RJ, Kimber MS, Bartlett DH, Rod Merrill A. Cholix toxin, a novel ADP-ribosylating factor from vibrio cholerae. J Biol Chem. 2008 Feb 25;. PMID:18276581 doi:M710008200
  2. ↑ Turgeon Z, White D, Jorgensen R, Visschedyk D, Fieldhouse RJ, Mangroo D, Merrill AR. Yeast as a tool for characterizing mono-ADP-ribosyltransferase toxins. FEMS Microbiol Lett. 2009 Nov;300(1):97-106. Epub 2009 Aug 31. PMID:19793133 doi:10.1111/j.1574-6968.2009.01777.x

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OCA

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