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| [[Image:2zjp.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2zjp.png|left|200px]] |
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| {{STRUCTURE_2zjp| PDB=2zjp | SCENE= }} | | {{STRUCTURE_2zjp| PDB=2zjp | SCENE= }} |
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| '''Thiopeptide antibiotic Nosiheptide bound to the large ribosomal subunit of Deinococcus radiodurans'''
| | ===Thiopeptide antibiotic Nosiheptide bound to the large ribosomal subunit of Deinococcus radiodurans=== |
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| ==Overview==
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| The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G, thus explaining how this class of drugs perturbs translation factor binding to the ribosome. The presence of Micro leads to additional density for the C-terminal domain (CTD) of L7, adjacent to and interacting with L11. The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G' subdomain of EF-G to regulate EF-G turnover during protein synthesis. | | The line below this paragraph, {{ABSTRACT_PUBMED_18406324}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18406324 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18406324}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zinc]] | | [[Category: Zinc]] |
| [[Category: Zinc-finger]] | | [[Category: Zinc-finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:07:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:08:48 2008'' |