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-A 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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| Enthalten in: |
Proceedings of the National Academy of Sciences of the United States of America - 106(2009), 22 vom: 02. Juni, Seite 8824-9 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sung, Ming-Ta [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 17.06.2009 Date Revised 20.10.2021 published: Print-Electronic PDB: 3FWL, 3FWM Citation Status MEDLINE |
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| doi: |
10.1073/pnas.0904030106 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM188673725 |
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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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| 500 | |a Date Completed 17.06.2009 | ||
| 500 | |a Date Revised 20.10.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a PDB: 3FWL, 3FWM | ||
| 500 | |a Citation Status MEDLINE | ||
| 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-A 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Enzyme Inhibitors |2 NLM | |
| 650 | 7 | |a Escherichia coli Proteins |2 NLM | |
| 650 | 7 | |a Oligosaccharides |2 NLM | |
| 650 | 7 | |a Penicillin-Binding Proteins |2 NLM | |
| 650 | 7 | |a Peptidoglycan Glycosyltransferase |2 NLM | |
| 650 | 7 | |a EC 2.4.1.129 |2 NLM | |
| 650 | 7 | |a penicillin-binding protein 1B, E coli |2 NLM | |
| 650 | 7 | |a EC 2.4.1.129 |2 NLM | |
| 650 | 7 | |a Serine-Type D-Ala-D-Ala Carboxypeptidase |2 NLM | |
| 650 | 7 | |a EC 3.4.16.4 |2 NLM | |
| 650 | 7 | |a moenomycin |2 NLM | |
| 650 | 7 | |a PP922A42V2 |2 NLM | |
| 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 | |
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| 773 | 1 | 8 | |g volume:106 |g year:2009 |g number:22 |g day:02 |g month:06 |g pages:8824-9 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1073/pnas.0904030106 |3 Volltext |
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