2XVA

Crystal structure of the tellurite detoxification protein TehB from E. coli in complex with sinefungin

Summary for 2XVA

• Entry DOI: 10.2210/pdb2xva/pdb
• Related: 2XVM
• Descriptor: TELLURITE RESISTANCE PROTEIN TEHB, SINEFUNGIN, ZINC ION, ... (4 entities in total)
• Functional Keywords: transferase
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm (Probable): P25397
• Total number of polymer chains: 4
• Total formula weight: 92421.14

Authors

Choudhury, H.G.,Cameron, A.D.,Iwata, S.,Beis, K. (deposition date: 2010-10-25, release date: 2011-02-16, Last modification date: 2023-12-20)

Primary citation

Choudhury, H.G.,Cameron, A.D.,Iwata, S.,Beis, K.
Structure and Mechanism of the Chalcogen Detoxifying Protein Tehb from Escherichia Coli.
Biochem.J., 435:85-, 2011

PubMed Abstract: The oxyanion derivatives of the chalcogens tellurium and selenium are toxic to living organisms even at very low levels. Bacteria have developed mechanisms to overcome their toxicity by methylating them. The structure of TehB from Escherichia coli has been determined in the presence of the cofactor analogues SAH (S-adenosylhomocysteine) and sinefungin (a non-hydrolysable form of S-adenosyl-L-methionine) at 1.48 Å (1 Å=0.1 nm) and 1.9 Å respectively. Interestingly, our kinetic data show that TehB does not discriminate between selenium or tellurite oxyanions, making it a very powerful detoxifying protein. Analysis of the active site has identified three conserved residues that are capable of binding and orientating the metals for nucleophilic attack: His176, Arg177 and Arg184. Mutagenesis studies revealed that the H176A and R184A mutants retained most of their activity, whereas the R177A mutant had 65% of its activity abolished. Based on the structure and kinetic data we propose an SN2 nucleophilic attack reaction mechanism. These data provide the first molecular understanding of the detoxification of chalcogens by bacteria.

PubMed: 21244361
DOI: 10.1042/BJ20102014

Experimental method

X-RAY DIFFRACTION (1.9 Å)