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PDBsum entry 2vl8
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* Residue conservation analysis
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Enzyme class 1:
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E.C.2.4.1.-
- ?????
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Enzyme class 2:
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E.C.3.4.22.-
- ?????
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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DOI no:
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Febs Lett
582:2277-2282
(2008)
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PubMed id:
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Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine.
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T.Jank,
M.O.Ziegler,
G.E.Schulz,
K.Aktories.
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ABSTRACT
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Castanospermine was identified as an inhibitor of the Rho/Ras-glucosylating
Clostridium sordellii lethal toxin and Clostridium difficile toxin B.
Microinjection of castanospermine into embryonic bovine lung cells prevented the
cytotoxic effects of toxins. The crystal structure of the glucosyltransferase
domain of C. sordellii lethal toxin in complex with castanospermine, UDP and a
calcium ion was solved at a resolution of 2.3A. The inhibitor binds in a
conformation that brings its four hydroxyl groups and its N-atom almost exactly
in the positions of the four hydroxyls and of the ring oxygen of the glucosyl
moiety of UDP-glucose, respectively.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Suwantarat,
and
D.A.Bobak
(2011).
Current Status of Nonantibiotic and Adjunct Therapies for Clostridium difficile Infection.
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Curr Infect Dis Rep,
13,
21-27.
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D.J.Wardrop,
and
S.L.Waidyarachchi
(2010).
Synthesis and biological activity of naturally occurring α-glucosidase inhibitors.
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Nat Prod Rep,
27,
1431-1468.
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P.Hookman,
and
J.S.Barkin
(2009).
Clostridium difficile associated infection, diarrhea and colitis.
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World J Gastroenterol,
15,
1554-1580.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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}
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