This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vq7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vq7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vq7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vq7| PDB=1vq7 | SCENE= }}
{{STRUCTURE_1vq7| PDB=1vq7 | SCENE= }}
-
'''The structure of the transition state analogue "DCA" bound to the large ribosomal subunit of haloarcula marismortui'''
+
===The structure of the transition state analogue "DCA" bound to the large ribosomal subunit of haloarcula marismortui===
-
==Overview==
+
<!--
-
The large ribosomal subunit catalyses the reaction between the alpha-amino group of the aminoacyl-tRNA bound to the A site and the ester carbon of the peptidyl-tRNA bound to the P site, while preventing the nucleophilic attack of water on the ester, which would lead to unprogrammed deacylation of the peptidyl-tRNA. Here we describe three new structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with peptidyl transferase substrate analogues that reveal an induced-fit mechanism in which substrates and active-site residues reposition to allow the peptidyl transferase reaction. Proper binding of an aminoacyl-tRNA analogue to the A site induces specific movements of 23S rRNA nucleotides 2618-2620 (Escherichia coli numbering 2583-2585) and 2541(2506), thereby reorienting the ester group of the peptidyl-tRNA and making it accessible for attack. In the absence of the appropriate A-site substrate, the peptidyl transferase centre positions the ester link of the peptidyl-tRNA in a conformation that precludes the catalysed nucleophilic attack by water. Protein release factors may also function, in part, by inducing an active-site rearrangement similar to that produced by the A-site aminoacyl-tRNA, allowing the carbonyl group and water to be positioned for hydrolysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16306996}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16306996 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16306996}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA., Schmeing TM, Huang KS, Strobel SA, Steitz TA, Nature. 2005 Nov 24;438(7067):520-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16306996 16306996]
An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA., Schmeing TM, Huang KS, Strobel SA, Steitz TA, Nature. 2005 Nov 24;438(7067):520-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16306996 16306996]
 +
 +
Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction., Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA, Mol Cell. 2005 Nov 11;20(3):437-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16285925 16285925]
[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 29: Line 35:
[[Category: Ribosome 50]]
[[Category: Ribosome 50]]
[[Category: Rna-rna complex]]
[[Category: Rna-rna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:47:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:54:58 2008''

Revision as of 16:55, 28 July 2008

Image:1vq7.png

Template:STRUCTURE 1vq7

The structure of the transition state analogue "DCA" bound to the large ribosomal subunit of haloarcula marismortui

Template:ABSTRACT PUBMED 16306996

About this Structure

1VQ7 is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.

Reference

An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA., Schmeing TM, Huang KS, Strobel SA, Steitz TA, Nature. 2005 Nov 24;438(7067):520-4. PMID:16306996

Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction., Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA, Mol Cell. 2005 Nov 11;20(3):437-48. PMID:16285925

Page seeded by OCA on Mon Jul 28 19:54:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vq7"
Personal tools