2jch
|
STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS
OverviewOverview
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 beta-lactam. Here we, show that LTV and a more potent analog, phenoxyacetyl-LTV (PLTV; 2), are, active against clinically isolated, penicillin-resistant Streptococcus, pneumoniae strains. Crystallographic analyses of S. pneumoniae PBP1b, reveal that LTV and PLTV inhibition involves opening of both ... [(full description)]
About this StructureAbout this Structure
2JCH is a [Single protein] structure of sequence from [Streptococcus pneumoniae (strain atcc baa-255 / r6)] with SO4, CL, EDO and PL7 as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins., Macheboeuf P, Fischer DS, Brown T Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ, Nat Chem Biol. 2007 Aug 5;. PMID:17676039
Page seeded by OCA on Mon Oct 29 17:32:59 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Single protein
- Streptococcus pneumoniae (strain atcc baa-255 / r6)
- Brown, T.J.
- Dessen, A.
- Fisher, D.S.
- Joris, B.
- Luxen, A.
- Macheboeuf, P.
- Schofield, C.J.
- Zervosen, A.
- CL
- EDO
- PL7
- SO4
- Binding protein
- Cell wall
- Drug-binding protein
- Gamma lactam antibiotics
- Peptidoglycan
- Peptidoglycan synthesis multifunctional enzyme