1vqp: Difference between revisions

Revision as of 13:12, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vqp.png

Template:STRUCTURE 1vqp

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

Template:ABSTRACT PUBMED 16285925

About this StructureAbout this Structure

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

ReferenceReference

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 Sun Jul 27 13:12:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1vqp.gif|left|200px]]
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 {{STRUCTURE_1vqp|  PDB=1vqp  |  SCENE=  }}
-'''The structure of the transition state analogue "RAP" bound to the large ribosomal subunit of haloarcula marismortui'''
+===The structure of the transition state analogue "RAP" bound to the large ribosomal subunit of haloarcula marismortui===
-==Overview==
+<!--
-Peptide bond formation is catalyzed at the peptidyl transferase center (PTC) of the large ribosomal subunit. Crystal structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with several analogs that represent either the substrates or the transition state intermediate of the peptidyl transferase reaction show that this reaction proceeds through a tetrahedral intermediate with S chirality. The oxyanion of the tetrahedral intermediate interacts with a water molecule that is positioned by nucleotides A2637 (E. coli numbering, 2602) and (methyl)U2619(2584). There are no Mg2+ ions or monovalent metal ions observed in the PTC that could directly promote catalysis. The A76 2' hydroxyl of the peptidyl-tRNA is hydrogen bonded to the alpha-amino group and could facilitate peptide bond formation by substrate positioning and by acting as a proton shuttle between the alpha-amino group and the A76 3' hydroxyl of the peptidyl-tRNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_16285925}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16285925 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16285925}}
 ==About this Structure==
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 [[Category: Ribosome 50]]
 [[Category: Rna-rna complex]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:12:53 2008''