1hq1
From Proteopedia
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- | [[Image:1hq1.gif|left|200px]] | + | [[Image:1hq1.gif|left|200px]] |
- | + | ||
- | '''STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE''' | + | {{Structure |
+ | |PDB= 1hq1 |SIZE=350|CAPTION= <scene name='initialview01'>1hq1</scene>, resolution 1.52Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1HQ1 is a [ | + | 1HQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQ1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11243816 11243816] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tetraloop]] | [[Category: tetraloop]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:07 2008'' |
Revision as of 09:40, 20 March 2008
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, resolution 1.52Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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