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  Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-β-lactamase: Structural flexibility without loss of activity

Rasia, R. M., Ceolin, M., & Vila, A. J. (2003). Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-β-lactamase: Structural flexibility without loss of activity. Protein Science, 12, 1538-1546. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2323933/pdf/0121538.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F1D1-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2C28-1
Genre: Journal Article

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 Creators:
Rasia, R. M.1, Author              
Ceolin, M.1, Author              
Vila, A. J., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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Free keywords: Metallo-(beta)-lactamase metal site engineering zinc enzyme metal substitution spectroscopy
 Abstract: Metallo-(beta)-lactamases are zinc enzymes able to hydrolyze the four-membered ring of (beta)-lactam antibiotics, representing one of the latest generations of (beta)-lactamases. These enzymes belong to the zinc metallohydrolase family of the (beta)-lactamase fold. Enzymes belonging to this family have a bimetallic active site whose structure varies among different members by point substitutions of the metal ligands. In this work, we have grafted new metal ligands into the metal binding site of BcII from Bacillus cereus that mimic the ligands present in other members of this superfamily. We have characterized spectroscopically and modeled the structure of the redesigned sites, which differ substantially from the wild-type enzyme. Despite the changes introduced in the active site, the mutant enzymes retain almost full activity. These results shed some light on the possible evolutionary origin of these metalloenzymes.

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Language(s): eng - English
 Dates: 2003
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 12 Sequence Number: - Start / End Page: 1538 - 1546 Identifier: -