2vhm

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{{STRUCTURE_2vhm| PDB=2vhm | SCENE= }}
{{STRUCTURE_2vhm| PDB=2vhm | SCENE= }}
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'''STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE RIBOSOME (PART 1 OF 4)'''
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===STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE RIBOSOME (PART 1 OF 4)===
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==Overview==
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Messenger-RNA-directed protein synthesis is accomplished by the ribosome. In eubacteria, this complex process is initiated by a specialized transfer RNA charged with formylmethionine (tRNA(fMet)). The amino-terminal formylated methionine of all bacterial nascent polypeptides blocks the reactive amino group to prevent unfavourable side-reactions and to enhance the efficiency of translation initiation. The first enzymatic factor that processes nascent chains is peptide deformylase (PDF); it removes this formyl group as polypeptides emerge from the ribosomal tunnel and before the newly synthesized proteins can adopt their native fold, which may bury the N terminus. Next, the N-terminal methionine is excised by methionine aminopeptidase. Bacterial PDFs are metalloproteases sharing a conserved N-terminal catalytic domain. All Gram-negative bacteria, including Escherichia coli, possess class-1 PDFs characterized by a carboxy-terminal alpha-helical extension. Studies focusing on PDF as a target for antibacterial drugs have not revealed the mechanism of its co-translational mode of action despite indications in early work that it co-purifies with ribosomes. Here we provide biochemical evidence that E. coli PDF interacts directly with the ribosome via its C-terminal extension. Crystallographic analysis of the complex between the ribosome-interacting helix of PDF and the ribosome at 3.7 A resolution reveals that the enzyme orients its active site towards the ribosomal tunnel exit for efficient co-translational processing of emerging nascent chains. Furthermore, we have found that the interaction of PDF with the ribosome enhances cell viability. These results provide the structural basis for understanding the coupling between protein synthesis and enzymatic processing of nascent chains, and offer insights into the interplay of PDF with the ribosome-associated chaperone trigger factor.
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(as it appears on PubMed at http://www.pubmed.gov), where 18288106 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18288106}}
==About this Structure==
==About this Structure==
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[[Category: Translation regulation]]
[[Category: Translation regulation]]
[[Category: Trna binding]]
[[Category: Trna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:49:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:27:42 2008''

Revision as of 17:27, 28 July 2008

Image:2vhm.png

Template:STRUCTURE 2vhm

STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE RIBOSOME (PART 1 OF 4)

Template:ABSTRACT PUBMED 18288106

About this Structure

2VHM is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing., Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antolic S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N, Nature. 2008 Feb 20;. PMID:18288106

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