1dt9: Difference between revisions

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-[[Image:1dt9.gif|left|200px]]<br />
+[[Image:1dt9.gif|left|200px]]<br /><applet load="1dt9" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1dt9" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1dt9, resolution 2.7&Aring;" />
 '''THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA HYDROLYSIS'''<br />
 ==Overview==
-The release factor eRF1 terminates protein biosynthesis by recognizing, stop codons at the A site of the ribosome and stimulating peptidyl-tRNA, bond hydrolysis at the peptidyl transferase center. The crystal structure, of human eRF1 to 2.8 A resolution, combined with mutagenesis analyses of, the universal GGQ motif, reveals the molecular mechanism of release factor, activity. The overall shape and dimensions of eRF1 resemble a tRNA, molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon, loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of, domain 2 suggests that the Gln residue coordinates a water molecule to, mediate the hydrolytic activity at the peptidyl transferase center. A, conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form, the codon recognition site.
+The release factor eRF1 terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase center. The crystal structure of human eRF1 to 2.8 A resolution, combined with mutagenesis analyses of the universal GGQ motif, reveals the molecular mechanism of release factor activity. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase center. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site.
 ==About this Structure==
-DT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DT9 OCA].
+DT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DT9 OCA].
 ==Reference==
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 [[Category: trna mimicry]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:14 2008''