First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

3fih

From Proteopedia

Jump to: navigation, search


3fih, resolution 6.70Å ()
Ligands:
Non-Standard Residues:
Related: 2i2u, 2i2v, 2j00, 1ob2, 3fik
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Ternary complex-bound E.coli 70S ribosome. This entry consists of the 30S subunit, tRNAs and the ternary complex.

Publication Abstract from PubMed

In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism.

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis., Villa E, Sengupta J, Trabuco LG, LeBarron J, Baxter WT, Shaikh TR, Grassucci RA, Nissen P, Ehrenberg M, Schulten K, Frank J, Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1063-8. Epub 2009 Jan 2. PMID:19122150

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3fih is a 26 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Villa E, Sengupta J, Trabuco LG, LeBarron J, Baxter WT, Shaikh TR, Grassucci RA, Nissen P, Ehrenberg M, Schulten K, Frank J. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1063-8. Epub 2009 Jan 2. PMID:19122150

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools