2zjp: Difference between revisions

Revision as of 04:08, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2zjp.png

Template:STRUCTURE 2zjp

Thiopeptide antibiotic Nosiheptide bound to the large ribosomal subunit of Deinococcus radioduransThiopeptide antibiotic Nosiheptide bound to the large ribosomal subunit of Deinococcus radiodurans

Template:ABSTRACT PUBMED 18406324

About this StructureAbout this Structure

2ZJP is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.

ReferenceReference

Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin., Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P, Mol Cell. 2008 Apr 11;30(1):26-38. PMID:18406324

Page seeded by OCA on Tue Jul 29 04:08:48 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
+<!--
-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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