2f2a

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(New page: 200px<br /><applet load="2f2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f2a, resolution 2.3&Aring;" /> '''Structure of tRNA-Dep...)
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[[Image:2f2a.gif|left|200px]]<br /><applet load="2f2a" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="2f2a, resolution 2.3&Aring;" />
'''Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln'''<br />
'''Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln'''<br />
==Overview==
==Overview==
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The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the, three domains of life. Most bacteria employ an indirect pathway to produce, Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB), that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of, crystal structures of intact GatCAB from Staphylococcus aureus in the apo, form and in the complexes with glutamine, asparagine, Mn2+, and adenosine, triphosphate analog. Two identified catalytic centers for the glutaminase, and transamidase reactions are markedly distant but connected by a, hydrophilic ammonia channel 30 A in length. Further, we show that the, first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve, as identity elements essential for discrimination by GatCAB and propose a, complete model for the overall concerted reactions to synthesize, Gln-tRNA(Gln).
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The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).
==About this Structure==
==About this Structure==
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2F2A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with MG and GLN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F2A OCA].
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2F2A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GLN:'>GLN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2A OCA].
==Reference==
==Reference==
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[[Category: trna]]
[[Category: trna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:18:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:58 2008''

Revision as of 15:16, 21 February 2008

Image:2f2a.gif

2f2a, resolution 2.3Å

Drag the structure with the mouse to rotate

Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln

Overview

The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).

About this Structure

2F2A is a Protein complex structure of sequences from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.

Reference

Ammonia channel couples glutaminase with transamidase reactions in GatCAB., Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I, Science. 2006 Jun 30;312(5782):1954-8. PMID:16809541

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