Crystal Structure of the Membrane-Bound Bifunctional Transglycosylase PBP1b from Escherichia Coli
Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-Å resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation..
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2009 |
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| Erschienen: |
2009 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:106 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sung, Ming-Ta [VerfasserIn] |
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| Links: |
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| Themen: |
Antibacterial development |
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| PPN (Katalog-ID): |
JST070347662 |
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| 100 | 1 | |a Sung, Ming-Ta |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Crystal Structure of the Membrane-Bound Bifunctional Transglycosylase PBP1b from Escherichia Coli |
| 264 | 1 | |c 2009 | |
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| 520 | |a Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-Å resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation. | ||
| 540 | |a Copyright 1993-2008 National Academy of Sciences of the United States of America | ||
| 650 | 4 | |a antibacterial development | |
| 650 | 4 | |a antibiotic resistance | |
| 650 | 4 | |a membrane protein structure | |
| 650 | 4 | |a peptidoglycan synthesis | |
| 650 | 4 | |a protein—protein interaction | |
| 650 | 4 | |a Biological sciences |x Biochemistry |x Biomolecules |x Macromolecules |x Lipids | |
| 650 | 4 | |a Physical sciences |x Physics |x Condensed matter physics |x Crystallography |x Crystal morphology |x Crystal structure | |
| 650 | 4 | |a Health sciences |x Medical sciences |x Pharmacology |x Clinical pharmacology |x Pharmacokinetics |x Drug interactions | |
| 650 | 4 | |a Biological sciences |x Biology |x Microbiology |x Bacteriology |x Bacteria |x Escherichia |x Escherichia coli | |
| 650 | 4 | |a Health sciences |x Medical sciences |x Pharmaceutics |x Pharmaceutical preparations |x Medications |x Antiinfectives |x Antibiotics | |
| 650 | 4 | |a Biological sciences |x Biology |x Cytology |x Cell biology |x Cellular structures |x Cell walls | |
| 650 | 4 | |a Biological sciences |x Biology |x Microbiology |x Bacteriology |x Bacteria | |
| 650 | 4 | |a Physical sciences |x Chemistry |x Chemical compounds |x Chemicals |x Polymers |x Biopolymers |x Proteins | |
| 650 | 4 | |a Physical sciences |x Physics |x Microphysics |x Molecular physics |x Molecular properties |x Molecular structure | |
| 650 | 4 | |a Physical sciences |x Physics |x Condensed matter physics |x Crystallography |x Crystals | |
| 650 | 4 | |a Biological sciences |x Biochemistry |x Biomolecules |x Macromolecules |x Lipids | |
| 650 | 4 | |a Physical sciences |x Physics |x Condensed matter physics |x Crystallography |x Crystal morphology |x Crystal structure | |
| 650 | 4 | |a Health sciences |x Medical sciences |x Pharmacology |x Clinical pharmacology |x Pharmacokinetics |x Drug interactions | |
| 650 | 4 | |a Biological sciences |x Biology |x Microbiology |x Bacteriology |x Bacteria |x Escherichia |x Escherichia coli | |
| 650 | 4 | |a Health sciences |x Medical sciences |x Pharmaceutics |x Pharmaceutical preparations |x Medications |x Antiinfectives |x Antibiotics | |
| 650 | 4 | |a Biological sciences |x Biology |x Cytology |x Cell biology |x Cellular structures |x Cell walls | |
| 650 | 4 | |a Biological sciences |x Biology |x Microbiology |x Bacteriology |x Bacteria | |
| 650 | 4 | |a Physical sciences |x Chemistry |x Chemical compounds |x Chemicals |x Polymers |x Biopolymers |x Proteins | |
| 650 | 4 | |a Physical sciences |x Physics |x Microphysics |x Molecular physics |x Molecular properties |x Molecular structure | |
| 650 | 4 | |a Physical sciences |x Physics |x Condensed matter physics |x Crystallography |x Crystals | |
| 655 | 4 | |a research-article | |
| 700 | 1 | |a Lai, Yen-Ting |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Chia-Ying |e verfasserin |4 aut | |
| 700 | 1 | |a Chou, Lien-Yang |e verfasserin |4 aut | |
| 700 | 1 | |a Shih, Hao-Wei |e verfasserin |4 aut | |
| 700 | 1 | |a Cheng, Wei-Chieh |e verfasserin |4 aut | |
| 700 | 1 | |a Wong, Chi-Huey |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Che |e verfasserin |4 aut | |
| 773 | 1 | 8 | |g volume:106 |g year:2009 |g number:22 |g pages:8824-8829 |
| 856 | 4 | 0 | |u https://www.jstor.org/stable/40482773 |3 Volltext |
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