1hr0: Difference between revisions

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New page: left|200px<br /><applet load="1hr0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hr0, resolution 3.20Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1hr0.jpg|left|200px]]<br /><applet load="1hr0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hr0.jpg|left|200px]]<br /><applet load="1hr0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hr0, resolution 3.20&Aring;" />
caption="1hr0, resolution 3.20&Aring;" />
'''CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT'''<br />
'''CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1HR0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with MG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HR0 OCA].  
1HR0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR0 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Brodersen, D.E.]]
[[Category: Brodersen, D E.]]
[[Category: Carter, A.P.]]
[[Category: Carter, A P.]]
[[Category: Jr., W.M.Clemons.]]
[[Category: Jr., W M.Clemons.]]
[[Category: Morgan-Warren, R.J.]]
[[Category: Morgan-Warren, R J.]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan, V.]]
[[Category: Wimberly, B.T.]]
[[Category: Wimberly, B T.]]
[[Category: MG]]
[[Category: MG]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: ribosome]]
[[Category: ribosome]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:46:01 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:59 2008''

Revision as of 14:04, 21 February 2008

File:1hr0.jpg


1hr0, resolution 3.20Å

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

OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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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