1zq1
From Proteopedia
(New page: 200px<br /><applet load="1zq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zq1, resolution 3.0Å" /> '''Structure of GatDE tR...) |
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| - | [[Image:1zq1.gif|left|200px]]<br /><applet load="1zq1" size=" | + | [[Image:1zq1.gif|left|200px]]<br /><applet load="1zq1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zq1, resolution 3.0Å" /> | caption="1zq1, resolution 3.0Å" /> | ||
'''Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi'''<br /> | '''Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Besides direct charging of tRNAs by aminoacyl-tRNA synthetases, indirect | + | Besides direct charging of tRNAs by aminoacyl-tRNA synthetases, indirect routes also ensure attachment of some amino acids onto tRNA. Such routes may explain how new amino acids entered into protein synthesis. In archaea and in most bacteria, tRNA(Gln) is first misaminoacylated by glutamyl-tRNA synthetase. Glu-tRNA(Gln) is then matured into Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report the structure of a tRNA-dependent amidotransferase-that of GatDE from Pyrococcus abyssi. The 3.0 A resolution crystal structure shows a tetramer with two GatD molecules as the core and two GatE molecules at the periphery. The fold of GatE cannot be related to that of any tRNA binding enzyme. The ammonium donor site on GatD and the tRNA site on GatE are markedly distant. Comparison of GatD and L-asparaginase structures shows how the motion of a beta hairpin region containing a crucial catalytic threonine may control the overall reaction cycle of GatDE. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with ASP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZQ1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray; 3d structure; asparaginase 1 family; gatd subfamily]] | [[Category: x-ray; 3d structure; asparaginase 1 family; gatd subfamily]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:59 2008'' |
Revision as of 14:17, 21 February 2008
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Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi
Overview
Besides direct charging of tRNAs by aminoacyl-tRNA synthetases, indirect routes also ensure attachment of some amino acids onto tRNA. Such routes may explain how new amino acids entered into protein synthesis. In archaea and in most bacteria, tRNA(Gln) is first misaminoacylated by glutamyl-tRNA synthetase. Glu-tRNA(Gln) is then matured into Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report the structure of a tRNA-dependent amidotransferase-that of GatDE from Pyrococcus abyssi. The 3.0 A resolution crystal structure shows a tetramer with two GatD molecules as the core and two GatE molecules at the periphery. The fold of GatE cannot be related to that of any tRNA binding enzyme. The ammonium donor site on GatD and the tRNA site on GatE are markedly distant. Comparison of GatD and L-asparaginase structures shows how the motion of a beta hairpin region containing a crucial catalytic threonine may control the overall reaction cycle of GatDE.
About this Structure
1ZQ1 is a Protein complex structure of sequences from Pyrococcus abyssi with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for tRNA-dependent amidotransferase function., Schmitt E, Panvert M, Blanquet S, Mechulam Y, Structure. 2005 Oct;13(10):1421-33. PMID:16216574
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