1hr0

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{{STRUCTURE_1hr0| PDB=1hr0 | SCENE= }}
{{STRUCTURE_1hr0| PDB=1hr0 | SCENE= }}
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'''CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT'''
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===CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT===
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==Overview==
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Initiation of translation at the correct position on messenger RNA is essential for accurate protein synthesis. In prokaryotes, this process requires three initiation factors: IF1, IF2, and IF3. Here we report the crystal structure of a complex of IF1 and the 30S ribosomal subunit. Binding of IF1 occludes the ribosomal A site and flips out the functionally important bases A1492 and A1493 from helix 44 of 16S RNA, burying them in pockets in IF1. The binding of IF1 causes long-range changes in the conformation of H44 and leads to movement of the domains of 30S with respect to each other. The structure explains how localized changes at the ribosomal A site lead to global alterations in the conformation of the 30S subunit.
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(as it appears on PubMed at http://www.pubmed.gov), where 11228145 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11228145}}
==About this Structure==
==About this Structure==
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[[Category: Ribosomal subunit]]
[[Category: Ribosomal subunit]]
[[Category: Ribosome]]
[[Category: Ribosome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:08:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:34:00 2008''

Revision as of 05:34, 1 July 2008

Image:1hr0.png

Template:STRUCTURE 1hr0

CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT

Template:ABSTRACT PUBMED 11228145

About this Structure

1HR0 is a Protein complex structure of sequences from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of an initiation factor bound to the 30S ribosomal subunit., Carter AP, Clemons WM Jr, Brodersen DE, Morgan-Warren RJ, Hartsch T, Wimberly BT, Ramakrishnan V, Science. 2001 Jan 19;291(5503):498-501. PMID:11228145

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