1hq1

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(New page: 200px<br /><applet load="1hq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hq1, resolution 1.52&Aring;" /> '''STRUCTURAL AND ENERG...)
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[[Image:1hq1.gif|left|200px]]<br /><applet load="1hq1" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hq1.gif|left|200px]]<br /><applet load="1hq1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hq1, resolution 1.52&Aring;" />
caption="1hq1, resolution 1.52&Aring;" />
'''STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE'''<br />
'''STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE'''<br />
==Overview==
==Overview==
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The signal recognition particle (SRP) is a ribonucleoprotein complex, responsible for targeting proteins to the endoplasmic reticulum in eukarya, or to the inner membrane in prokarya. The crystal structure of the, universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the, 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops, create a unique surface for protein recognition. To determine the, energetic importance of conserved nucleotides for SRP assembly, we, measured the affinity of the M domain for a series of RNA mutants. This, analysis reveals how conserved nucleotides within the two internal loop, motifs establish the architecture of the macromolecular interface and, position essential functional groups for direct recognition by the, protein.
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The signal recognition particle (SRP) is a ribonucleoprotein complex responsible for targeting proteins to the endoplasmic reticulum in eukarya or to the inner membrane in prokarya. The crystal structure of the universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops create a unique surface for protein recognition. To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants. This analysis reveals how conserved nucleotides within the two internal loop motifs establish the architecture of the macromolecular interface and position essential functional groups for direct recognition by the protein.
==About this Structure==
==About this Structure==
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1HQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and K as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQ1 OCA].
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1HQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQ1 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Batey, R.T.]]
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[[Category: Batey, R T.]]
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[[Category: Doudna, J.A.]]
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[[Category: Doudna, J A.]]
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[[Category: Sagar, M.B.]]
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[[Category: Sagar, M B.]]
[[Category: K]]
[[Category: K]]
[[Category: MG]]
[[Category: MG]]
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[[Category: tetraloop]]
[[Category: tetraloop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:44:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:41 2008''

Revision as of 11:03, 21 February 2008


1hq1, resolution 1.52Å

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STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE

Overview

The signal recognition particle (SRP) is a ribonucleoprotein complex responsible for targeting proteins to the endoplasmic reticulum in eukarya or to the inner membrane in prokarya. The crystal structure of the universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops create a unique surface for protein recognition. To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants. This analysis reveals how conserved nucleotides within the two internal loop motifs establish the architecture of the macromolecular interface and position essential functional groups for direct recognition by the protein.

About this Structure

1HQ1 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle., Batey RT, Sagar MB, Doudna JA, J Mol Biol. 2001 Mar 16;307(1):229-46. PMID:11243816

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