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Journal article

Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins.

Abstract:

Beta-lactam antibiotics, including penicillins and cephalosporins, inhibit penicillin-binding proteins (PBPs), which are essential for bacterial cell wall biogenesis. Pathogenic bacteria have evolved efficient antibiotic resistance mechanisms that, in Gram-positive bacteria, include mutations to PBPs that enable them to avoid beta-lactam inhibition. Lactivicin (LTV; 1) contains separate cycloserine and gamma-lactone rings and is the only known natural PBP inhibitor that does not contain a bet...

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Publication status:
Published

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Publisher copy:
10.1038/nchembio.2007.21

Authors


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Journal:
Nature chemical biology
Volume:
3
Issue:
9
Pages:
565-569
Publication date:
2007-09-01
DOI:
EISSN:
1552-4469
ISSN:
1552-4450
Source identifiers:
40495
Language:
English
Keywords:
Pubs id:
pubs:40495
UUID:
uuid:d25c8e61-dfdc-46f4-87d8-a03bf43c5961
Local pid:
pubs:40495
Deposit date:
2012-12-19

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