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1vqn

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[[Image:1vqn.gif|left|200px]]
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{{STRUCTURE_1vqn| PDB=1vqn | SCENE= }}
{{STRUCTURE_1vqn| PDB=1vqn | SCENE= }}
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'''The structure of CC-HPMN AND CCA-PHE-CAP-BIO bound to the large ribosomal subunit of haloarcula marismortui'''
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===The structure of CC-HPMN AND CCA-PHE-CAP-BIO bound to the large ribosomal subunit of haloarcula marismortui===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16306996}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16306996 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16306996}}
==About this Structure==
==About this Structure==
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==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]
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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]]
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[[Category: Ribosome 50]]
[[Category: Ribosome 50]]
[[Category: Rna-rna complex]]
[[Category: Rna-rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:48:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:13:27 2008''

Revision as of 10:13, 29 July 2008

Image:1vqn.png

Template:STRUCTURE 1vqn

The structure of CC-HPMN AND CCA-PHE-CAP-BIO bound to the large ribosomal subunit of haloarcula marismortui

Template:ABSTRACT PUBMED 16306996

About this Structure

1VQN 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 Tue Jul 29 13:13:27 2008

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