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Sandbox Reserved 1488

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Revision as of 13:30, 10 January 2019

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

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Enterococcus faecalis Penicillin Binding Protein 4 (PBP4)

Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria^[1].

1 Function
2 Disease
3 Structure
4 Structural insights into β-lactam resistance

Function

The bacterial cell wall is essential for cell survival. It is composed of layers of peptidoglycan modified with proteins and polymers. In bacteria, this peptidoglycan layer is formed by the coordinated action of multiple proteins, including penicillin-binding proteins (PBPs). PBPs are transpeptidases, carboxypeptidases and endopeptidases that synthesize new and remodel existing peptidoglycan.

PBPs are classified by their enzymatic activity:

(1) class A, bifunctional PBPs with both glycosyltransferase and transpeptidase activities;

(2) class B, transpeptidases; and

(3) class C, carboxy-peptidases and endopeptidases.

Disease

Enterococci exhibits tolerance to the bactericidal activity of β-lactams ^[2] , a phenomenon that compromises the use of β-lactam antibiotics as single agents in the treatment of enterococcal endocarditis ^[3]. As a consequence, multi-resistant E. faecium and E. faecalis represent one of the most dangerous threats in infectious diseases therapeutics.

Rare strains of E. faecalis and most nosocomial strains of E. faecium exhibit even higher levels of resistance to penicillins, effectively eliminating β-lactams as a treatment option ^[4]. Of greater concern is the observation that prolonged β-lactam therapy can lead to the emergence of highly resistant strains.

Structure

Structural insights into β-lactam resistance

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

↑ Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P. The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev. 2008 Mar;32(2):234-58. doi: 10.1111/j.1574-6976.2008.00105.x., Epub 2008 Feb 11. PMID:18266856 doi:http://dx.doi.org/10.1111/j.1574-6976.2008.00105.x
↑ Moellering RC Jr, Weinberg AN. Studies on antibiotic syngerism against enterococci. II. Effect of various antibiotics on the uptake of 14 C-labeled streptomycin by enterococci. J Clin Invest. 1971 Dec;50(12):2580-4. doi: 10.1172/JCI106758. PMID:5001959 doi:http://dx.doi.org/10.1172/JCI106758
↑ Jawetz E, Sonne M. Penicillin-streptomycin treatment of enterococcal endocarditis. A re-evaluation. N Engl J Med. 1966 Mar 31;274(13):710-5. doi: 10.1056/NEJM196603312741304. PMID:5908873 doi:http://dx.doi.org/10.1056/NEJM196603312741304
↑ Rice LB. Federal funding for the study of antimicrobial resistance in nosocomial pathogens: no ESKAPE. J Infect Dis. 2008 Apr 15;197(8):1079-81. doi: 10.1086/533452. PMID:18419525 doi:http://dx.doi.org/10.1086/533452

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1488"

@@ Line 2: / Line 2: @@
 ==Enterococcus faecalis Penicillin Binding Protein 4 (PBP4)==
 <StructureSection load='6bsq' size='340' side='right' caption='Caption for this structure' scene=''>
-This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria<ref>DOI:10.1111/j.1574-6976.2008.00105.x</ref>.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 ==Function ==
@@ Line 10: / Line 10: @@
 PBPs are classified by their enzymatic activity:
 (1)  class A, bifunctional PBPs with both glycosyltransferase and transpeptidase activities;
 (2)  class B, transpeptidases; and
 (3)  class C, carboxy-peptidases and endopeptidases.
 == Disease ==
+Enterococci exhibits tolerance to the bactericidal activity of β-lactams <ref>DOI:10.1172/JCI106758</ref> , a phenomenon that compromises the use of β-lactam antibiotics as single agents in the treatment of enterococcal endocarditis <ref>DOI: 10.1056/NEJM196603312741304</ref>. As a consequence, multi-resistant E. faecium and E. faecalis represent one of the most dangerous threats in infectious diseases therapeutics.
+Rare strains of E. faecalis and most nosocomial strains of E. faecium exhibit even higher levels of resistance to penicillins, effectively eliminating β-lactams as a treatment option <ref>doi: 10.1086/533452</ref>. Of greater concern is the observation that prolonged β-lactam therapy can lead to the emergence of highly resistant strains.
 == Structure ==

Sandbox Reserved 1488

From Proteopedia

Revision as of 13:30, 10 January 2019

Enterococcus faecalis Penicillin Binding Protein 4 (PBP4)

Contents

Function

Disease

Structure

Structural insights into β-lactam resistance

References

Views

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