1xzp
From Proteopedia
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- | [[Image:1xzp.gif|left|200px]] | + | [[Image:1xzp.gif|left|200px]] |
- | + | ||
- | '''Structure of the GTP-binding protein TrmE from Thermotoga maritima''' | + | {{Structure |
+ | |PDB= 1xzp |SIZE=350|CAPTION= <scene name='initialview01'>1xzp</scene>, resolution 2.3Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= TrmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
+ | }} | ||
+ | |||
+ | '''Structure of the GTP-binding protein TrmE from Thermotoga maritima''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1XZP is a [ | + | 1XZP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15616586 15616586] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: trna-modification]] | [[Category: trna-modification]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:16:37 2008'' |
Revision as of 13:16, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | |||||||
Gene: | TrmE (Thermotoga maritima) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 15:16:37 2008