1f27

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(New page: 200px<br /> <applet load="1f27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f27, resolution 1.30&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF A BIOTIN-BINDING RNA PSEUDOKNOT'''<br />
'''CRYSTAL STRUCTURE OF A BIOTIN-BINDING RNA PSEUDOKNOT'''<br />
==Overview==
==Overview==
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A pseudoknot-containing aptamer isolated from a pool of random sequence, molecules has been shown previously to represent an optimal RNA solution, to the problem of binding biotin. The affinity of this RNA molecule is, nonetheless orders of magnitude weaker than that of its highly evolved, protein analogs, avidin and streptavidin. To understand the structural, basis for biotin binding and to compare directly strategies for ligand, recognition available to proteins and RNA molecules, we have determined, the 1.3 A crystal structure of the aptamer complexed with its ligand., Biotin is bound at the interface between the pseudoknot's stacked helices, in a pocket defined almost entirely by base-paired nucleotides. In, comparison to the protein avidin, the aptamer packs more tightly around, the biotin headgroup and makes fewer contacts with its fatty acid tail., Whereas biotin is deeply buried within the hydrophobic core in the avidin, complex, the aptamer relies on a combination of hydrated magnesium ions, and immobilized water molecules to surround its ligand. In addition to, demonstrating fundamentally different approaches to molecular recognition, by proteins and RNA, the structure provides general insight into the, mechanisms by which RNA function is mediated by divalent metals.
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A pseudoknot-containing aptamer isolated from a pool of random sequence molecules has been shown previously to represent an optimal RNA solution to the problem of binding biotin. The affinity of this RNA molecule is nonetheless orders of magnitude weaker than that of its highly evolved protein analogs, avidin and streptavidin. To understand the structural basis for biotin binding and to compare directly strategies for ligand recognition available to proteins and RNA molecules, we have determined the 1.3 A crystal structure of the aptamer complexed with its ligand. Biotin is bound at the interface between the pseudoknot's stacked helices in a pocket defined almost entirely by base-paired nucleotides. In comparison to the protein avidin, the aptamer packs more tightly around the biotin headgroup and makes fewer contacts with its fatty acid tail. Whereas biotin is deeply buried within the hydrophobic core in the avidin complex, the aptamer relies on a combination of hydrated magnesium ions and immobilized water molecules to surround its ligand. In addition to demonstrating fundamentally different approaches to molecular recognition by proteins and RNA, the structure provides general insight into the mechanisms by which RNA function is mediated by divalent metals.
==About this Structure==
==About this Structure==
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1F27 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with MG and BTN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F27 OCA].
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1F27 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=BTN:'>BTN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F27 OCA].
==Reference==
==Reference==
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[[Category: rna aptamer]]
[[Category: rna aptamer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 12:39:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:57 2008''

Revision as of 10:33, 21 February 2008


1f27, resolution 1.30Å

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CRYSTAL STRUCTURE OF A BIOTIN-BINDING RNA PSEUDOKNOT

Overview

A pseudoknot-containing aptamer isolated from a pool of random sequence molecules has been shown previously to represent an optimal RNA solution to the problem of binding biotin. The affinity of this RNA molecule is nonetheless orders of magnitude weaker than that of its highly evolved protein analogs, avidin and streptavidin. To understand the structural basis for biotin binding and to compare directly strategies for ligand recognition available to proteins and RNA molecules, we have determined the 1.3 A crystal structure of the aptamer complexed with its ligand. Biotin is bound at the interface between the pseudoknot's stacked helices in a pocket defined almost entirely by base-paired nucleotides. In comparison to the protein avidin, the aptamer packs more tightly around the biotin headgroup and makes fewer contacts with its fatty acid tail. Whereas biotin is deeply buried within the hydrophobic core in the avidin complex, the aptamer relies on a combination of hydrated magnesium ions and immobilized water molecules to surround its ligand. In addition to demonstrating fundamentally different approaches to molecular recognition by proteins and RNA, the structure provides general insight into the mechanisms by which RNA function is mediated by divalent metals.

About this Structure

1F27 is a Protein complex structure of sequences from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

The 1.3 A crystal structure of a biotin-binding pseudoknot and the basis for RNA molecular recognition., Nix J, Sussman D, Wilson C, J Mol Biol. 2000 Mar 10;296(5):1235-44. PMID:10698630

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