2a8k

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(New page: 200px<br /><applet load="2a8k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a8k, resolution 1.5&Aring;" /> '''Structural and Mutati...)
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[[Image:2a8k.gif|left|200px]]<br /><applet load="2a8k" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Structural and Mutational Studies of the Catalytic Domain of Colicin E5a tRNA-Specific Ribonuclease'''<br />
'''Structural and Mutational Studies of the Catalytic Domain of Colicin E5a tRNA-Specific Ribonuclease'''<br />
==Overview==
==Overview==
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Colicin E5 specifically cleaves four tRNAs in Escherichia coli that, contain the modified nucleotide queuosine (Q) at the wobble position, thereby preventing protein synthesis and ultimately resulting in cell, death. Here, the crystal structure of the catalytic domain of colicin E5, (E5-CRD) from E. coli was determined at 1.5 A resolution. Unexpectedly, E5-CRD adopts a core folding with a four-stranded beta-sheet packed, against an alpha-helix, seen in the well-studied ribonuclease T1 despite a, lack of sequence similarity. Beyond the core catalytic domain, an, N-terminal helix, a C-terminal beta-strand and loop, and an extended, internal loop constitute an RNA binding cleft. Mutational analysis, identified five amino acids that were important for tRNA substrate binding, and cleavage by E5-CRD. The structure, together with the mutational study, allows us to propose a model of colicin E5-tRNA interactions, suggesting, the molecular basis of tRNA substrate recognition and the mechanism of, tRNA cleavage by colicin E5.
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Colicin E5 specifically cleaves four tRNAs in Escherichia coli that contain the modified nucleotide queuosine (Q) at the wobble position, thereby preventing protein synthesis and ultimately resulting in cell death. Here, the crystal structure of the catalytic domain of colicin E5 (E5-CRD) from E. coli was determined at 1.5 A resolution. Unexpectedly, E5-CRD adopts a core folding with a four-stranded beta-sheet packed against an alpha-helix, seen in the well-studied ribonuclease T1 despite a lack of sequence similarity. Beyond the core catalytic domain, an N-terminal helix, a C-terminal beta-strand and loop, and an extended internal loop constitute an RNA binding cleft. Mutational analysis identified five amino acids that were important for tRNA substrate binding and cleavage by E5-CRD. The structure, together with the mutational study, allows us to propose a model of colicin E5-tRNA interactions, suggesting the molecular basis of tRNA substrate recognition and the mechanism of tRNA cleavage by colicin E5.
==About this Structure==
==About this Structure==
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2A8K 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 CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A8K OCA].
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2A8K 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=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8K OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Elias, Y.]]
[[Category: Elias, Y.]]
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[[Category: Huang, R.H.]]
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[[Category: Huang, R H.]]
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[[Category: Lin, Y.L.]]
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[[Category: Lin, Y L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: ribonuclease]]
[[Category: ribonuclease]]
[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:59:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:40 2008''

Revision as of 14:24, 21 February 2008


2a8k, resolution 1.5Å

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Structural and Mutational Studies of the Catalytic Domain of Colicin E5a tRNA-Specific Ribonuclease

Overview

Colicin E5 specifically cleaves four tRNAs in Escherichia coli that contain the modified nucleotide queuosine (Q) at the wobble position, thereby preventing protein synthesis and ultimately resulting in cell death. Here, the crystal structure of the catalytic domain of colicin E5 (E5-CRD) from E. coli was determined at 1.5 A resolution. Unexpectedly, E5-CRD adopts a core folding with a four-stranded beta-sheet packed against an alpha-helix, seen in the well-studied ribonuclease T1 despite a lack of sequence similarity. Beyond the core catalytic domain, an N-terminal helix, a C-terminal beta-strand and loop, and an extended internal loop constitute an RNA binding cleft. Mutational analysis identified five amino acids that were important for tRNA substrate binding and cleavage by E5-CRD. The structure, together with the mutational study, allows us to propose a model of colicin E5-tRNA interactions, suggesting the molecular basis of tRNA substrate recognition and the mechanism of tRNA cleavage by colicin E5.

About this Structure

2A8K is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structural and mutational studies of the catalytic domain of colicin E5: a tRNA-specific ribonuclease., Lin YL, Elias Y, Huang RH, Biochemistry. 2005 Aug 9;44(31):10494-500. PMID:16060658

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