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1xzp
From Proteopedia
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[[Image:1xzp.gif|left|200px]] | [[Image:1xzp.gif|left|200px]] | ||
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'''Structure of the GTP-binding protein TrmE from Thermotoga maritima''' | '''Structure of the GTP-binding protein TrmE from Thermotoga maritima''' | ||
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[[Category: Vetter, I R.]] | [[Category: Vetter, I R.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: | + | [[Category: Gtp-binding]] |
| - | [[Category: | + | [[Category: Thf-binding]] |
| - | [[Category: | + | [[Category: Trna-modification]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:42:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:42, 3 May 2008
Structure of the GTP-binding protein TrmE from Thermotoga maritima
Overview
TrmE is a 50 kDa guanine nucleotide-binding protein conserved between bacteria and man. It is involved in the modification of uridine bases (U34) at the first anticodon (wobble) position of tRNAs decoding two-family box triplets. The precise role of TrmE in the modification reaction is hitherto unknown. Here, we report the X-ray structure of TrmE from Thermotoga maritima. The structure reveals a three-domain protein comprising the N-terminal alpha/beta domain, the central helical domain and the G domain, responsible for GTP binding and hydrolysis. The N-terminal domain induces dimerization and is homologous to the tetrahydrofolate-binding domain of N,N-dimethylglycine oxidase. Biochemical and structural studies show that TrmE indeed binds formyl-tetrahydrofolate. A cysteine residue, necessary for modification of U34, is located close to the C1-group donor 5-formyl-tetrahydrofolate, suggesting a direct role of TrmE in the modification analogous to DNA modification enzymes. We propose a reaction mechanism whereby TrmE actively participates in the formylation reaction of uridine and regulates the ensuing hydrogenation reaction of a Schiff's base intermediate.
About this Structure
1XZP is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
The structure of the TrmE GTP-binding protein and its implications for tRNA modification., Scrima A, Vetter IR, Armengod ME, Wittinghofer A, EMBO J. 2005 Jan 12;24(1):23-33. Epub 2004 Dec 16. PMID:15616586 Page seeded by OCA on Sat May 3 15:42:32 2008
