Sandbox Reserved 307: Difference between revisions
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EF-Tu binds an aminoacylated tRNA molecule and allows entry into the ribosome <ref name="gp"/>. The tRNA anticodon associates with the mRNA codon in the A site of the ribosome. If the pairing is incorrect, the tRNA will likely leave the ribosome. However, if a correct pairing has occurred, EF-Tu hydrolyzes guanosine triphosphate (GTP) to the diphosphate form (GDP)<ref name="gp"/>. This hydrolysis results in a change in conformation of the tRNA, which allows it to dissociate from EF-Tu. The dissociation allows the tRNA molecule to then completely interact with the A site of the ribosome the tRNA can be transferred to the growing peptide chain via covalent bond formation <ref name="gp"/>. In this way, EF-Tu is a vital component in the propcess of lengthening a peptide during protein synthesis. | EF-Tu binds an aminoacylated tRNA molecule and allows entry into the ribosome <ref name="gp"/>. The tRNA anticodon associates with the mRNA codon in the A site of the ribosome. If the pairing is incorrect, the tRNA will likely leave the ribosome. However, if a correct pairing has occurred, EF-Tu hydrolyzes guanosine triphosphate (GTP) to the diphosphate form (GDP)<ref name="gp"/>. This hydrolysis results in a change in conformation of the tRNA, which allows it to dissociate from EF-Tu. The dissociation allows the tRNA molecule to then completely interact with the A site of the ribosome the tRNA can be transferred to the growing peptide chain via covalent bond formation <ref name="gp"/>. In this way, EF-Tu is a vital component in the propcess of lengthening a peptide during protein synthesis. | ||
EF-Tu has also been shown to play a role in the inhibition of tetracycline during protein synthesis in many different organisms <ref name="gp"/>. EF-Tu may be a target protein of tetracycline <ref name="gp"/>. | EF-Tu has also been shown to play a role in the inhibition of tetracycline during protein synthesis in many different organisms <ref name="gp"/>. EF-Tu may be a target protein of tetracycline, although this idea has commonly been dismissed because the ribosome may be inhibited in the presence of the antibiotic <ref name="gp"/>. Now however, it has been demonstated that Tm-EF-Tu-MgGDP is bound in a complex during crystallization, binding the the GTPase active site. This information could be useful for developing mechanisms of counteracting resistance to this particular antibiotic <ref name="gp"/>. | ||
==References== | ==References== | ||
<references/> | <references/> | ||