A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics (Q27642990)

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English	A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics	scientific article

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scholarly article

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A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics (English)

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Streptococcus pneumoniae

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based on heuristic

inferred from title

7

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6

object named as

Otto Dideberg

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Laurent Chesnel

2

object named as

Laurent Chesnel

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author name string

Lucile Pernot

1

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Laurent Chesnel

2

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Audrey Le Gouellec

3

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Jacques Croizé

4

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Thierry Vernet

5

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language of work or name

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publication date

16 April 2004

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Journal of Biological Chemistry

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279

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16

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16463-70

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Resistance among Streptococcus pneumoniae: Implications for drug selection

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Geographic diversity and temporal trends of antimicrobial resistance in Streptococcus pneumoniae in the United States.

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Assembly of the monomer unit of bacterial peptidoglycan.

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Molecular structures of penicillin-binding proteins and beta-lactamases

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The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains

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Serine beta-lactamases and penicillin-binding proteins

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Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with beta-lactams

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Penicillin-binding proteins and the mechanism of action of beta-lactam antibiotics

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Horizontal transfer of multiple penicillin-binding protein genes, and capsular biosynthetic genes, in natural populations of Streptococcus pneumoniae.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Analysis of penicillin-binding protein genes of clinical isolates of Streptococcus pneumoniae with reduced susceptibility to amoxicillin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Effects of amino acid alterations in penicillin-binding proteins (PBPs) 1a, 2b, and 2x on PBP affinities of penicillin, ampicillin, amoxicillin, cefditoren, cefuroxime, cefprozil, and cefaclor in 18 clinical isolates of penicillin-susceptible, -inte

1 reference

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Five independent combinations of mutations can result in low-affinity penicillin-binding protein 2x of Streptococcus pneumoniae

1 reference

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Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae

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Genome of the Bacterium Streptococcus pneumoniae Strain R6

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Biochemical characterization of penicillin-resistant and -sensitive penicillin-binding protein 2x transpeptidase activities of Streptococcus pneumoniae and mechanistic implications in bacterial resistance to beta-lactam antibiotics

1 reference

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Kinetic and mechanistic studies of penicillin-binding protein 2x from Streptococcus pneumoniae

1 reference

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The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance

1 reference

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Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations

1 reference

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X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

1 reference

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Mutations in the active site of penicillin-binding protein PBP2x from Streptococcus pneumoniae. Role in the specificity for beta-lactam antibiotics.

1 reference

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Identification of a structural determinant for resistance to beta-lactam antibiotics in Gram-positive bacteria

1 reference

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The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

21 January 2018

Integration of macromolecular diffraction data

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https://api.crossref.org/works/10.1074%2FJBC.M313492200

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The CCP4 suite: programs for protein crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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AMoRe: an automated package for molecular replacement

1 reference

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

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Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Kinetics of Interaction between the Exocellular DD‐Carboxypeptidase‐Transpeptidase from Streptomyces R61 and β‐Lactam Antibiotics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Mosaic genes and mosaic chromosomes: intra- and interspecies genomic variation of Streptococcus pneumoniae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

21 January 2018

The 2.4-A crystal structure of the penicillin-resistant penicillin-binding protein PBP5fm from Enterococcus faecium in complex with benzylpenicillin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313492200

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Raster3D Version 2.0. A program for photorealistic molecular graphics

1 reference

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Antibodies against the benzylpenicilloyl moiety as a probe for penicillin-binding proteins

1 reference

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Penicillin-binding proteins 2x and 2b as primary PBP targets in Streptococcus pneumoniae

1 reference

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Deacylation kinetics analysis of Streptococcus pneumoniae penicillin-binding protein 2x mutants resistant to beta-lactam antibiotics using electrospray ionization- mass spectrometry

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https://api.crossref.org/works/10.1074%2FJBC.M313492200

21 January 2018

Identifiers

10.1074/JBC.M313492200

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