PDBsum entry: 2vl8

Toxin

PDB-id: 2vl8

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Description

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References

PROCHECK

Protein chains

539 a.a. *

Ligands

UDP ×3

CTS ×3

Metal ions

_CA ×5

Waters ×400

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

2vl8

Name:

Toxin

Title:

Crystal structure of the catalytic domain of lethal toxin from clostridium sordellii in complex with udp, castanospermine and calcium ion

Structure:

Cytotoxin l. Chain: a, b, c. Fragment: catalytic domain, residues 1-546. Engineered: yes. Mutation: yes

Source:

Clostridium sordellii. Organism_taxid: 1505. Strain: 6018. Expressed in: escherichia coli. Expression_system_taxid: 562

UniProt:

Chains A, B, C: Q46342 (Q46342_CLOSO)

Seq:

Struc:

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Struc:

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Struc:

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Struc:

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Struc:

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Struc:

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Struc:

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Struc:

Seq:

Struc:

Seq:

2364 a.a.

Struc:

539 a.a.*

Key:	PfamA domain	PfamB domain
Secondary structure

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Resolution:

2.31Å

R-factor:

0.218

R-free:

0.255

Authors:

T.Jank,M.O.P.Ziegler,G.E.Schulz,K.Aktories

Key ref:

T.Jank et al. (2008). Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine.. Febs Lett, 582, 2277-2282. [PubMed id: 18505687] [DOI: 10.1016/j.febslet.2008.05.025]

Date:

09-Jan-08

Release date:

17-Jun-08

Related entries:

2vkh crystal structure of the catalytic domain of lethal toxin from clostridium sordellii in complex with udp-glc and calcium ion
2vkd crystal structure of the catalytic domain of lethal toxin from clostridium sordellii in complex with udp-glc and manganese ion

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Key reference

DOI no: 10.1016/j.febslet.2008.05.025

Febs Lett 582:2277-2282 (2008)

PubMed id: 18505687

Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine.

T.Jank, M.O.Ziegler, G.E.Schulz, K.Aktories.

ABSTRACT

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.