2df4: Difference between revisions

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New page: left|200px<br /><applet load="2df4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2df4, resolution 3.2Å" /> '''Structure of tRNA-Dep...
 
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[[Image:2df4.gif|left|200px]]<br /><applet load="2df4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2df4.gif|left|200px]]<br /><applet load="2df4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2df4, resolution 3.2&Aring;" />
caption="2df4, resolution 3.2&Aring;" />
'''Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Mn2+'''<br />
'''Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Mn2+'''<br />


==Overview==
==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).
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==
2DF4 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DF4 OCA].  
2DF4 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF4 OCA].  


==Reference==
==Reference==
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[[Category: multi protein complex]]
[[Category: multi protein complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:34:35 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:18 2008''

Revision as of 17:58, 21 February 2008

File:2df4.gif


2df4, resolution 3.2Å

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Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Mn2+

OverviewOverview

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 StructureAbout this Structure

2DF4 is a Protein complex structure of sequences from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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