Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae. - Wikidata - awgldk - TriplyDB

Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.

Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.

http://www.wikidata.org/entity/Q34561860

about

Stress Physiology of Lactic Acid Bacteria Recent advances in pneumococcal peptidoglycan biosynthesis suggest new vaccine and antimicrobial targets How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis The biofilm inhibitor carolacton disturbs membrane integrity and cell division of Streptococcus mutans through the serine/threonine protein kinase PknB.Reciprocal regulation of cephalosporin resistance in Enterococcus faecalis.A Serine-Threonine Kinase (StkP) Regulates Expression of the Pneumococcal Pilus and Modulates Bacterial Adherence to Human Epithelial and Endothelial Cells In Vitro.The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP Messenger functions of the bacterial cell wall-derived muropeptides.The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces.The external PASTA domain of the essential serine/threonine protein kinase PknB regulates mycobacterial growth Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance.Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?How to get (a)round: mechanisms controlling growth and division of coccoid bacteria.Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.Distribution of PASTA domains in penicillin-binding proteins and serine/threonine kinases of Actinobacteria.β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Pentapeptide-rich peptidoglycan at the Bacillus subtilis cell-division site.Regulation of bacterial cell wall growth.Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.Growth- and stress-induced PASTA kinase phosphorylation in Enterococcus faecalis.Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.Carolacton Treatment Causes Delocalization of the Cell Division Proteins PknB and DivIVa in Streptococcus mutans in vivo.Phosphorylation of the Streptococcus pneumoniae cell wall biosynthesis enzyme MurC by a eukaryotic-like Ser/Thr kinase.PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.Interaction of Penicillin-Binding Protein 2x and Ser/Thr protein kinase StkP, two key players in Streptococcus pneumoniae R6 morphogenesis.Identification of EloR (Spr1851) as a regulator of cell elongation in Streptococcus pneumoniae.Dual regulation of activity and intracellular localization of the PASTA kinase PrkC during Bacillus subtilis growth.Phosphorylation-dependent activation of the cell wall synthase PBP2a in Streptococcus pneumoniae by MacP.Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae.Structural and dynamic features of PASTA domains with different functional roles.

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Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.

http://www.wikidata.org/entity/Q34561860

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2010 nî lūn-bûn

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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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J.FEBSLET.2010.12.016

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Recognition of peptidoglycan a ...... from Streptococcus pneumoniae.

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P2860

Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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

The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation

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

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

Multiple enzymatic activities of the murein hydrolase from staphylococcal phage phi11. Identification of a D-alanyl-glycine endopeptidase activity

Two-component signal transduction

Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB

A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments

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