1xzp
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1xzp |SIZE=350|CAPTION= <scene name='initialview01'>1xzp</scene>, resolution 2.3Å | |PDB= 1xzp |SIZE=350|CAPTION= <scene name='initialview01'>1xzp</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TrmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |GENE= TrmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xzq|1XZQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xzp OCA], [http://www.ebi.ac.uk/pdbsum/1xzp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xzp RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Vetter, I R.]] | [[Category: Vetter, I R.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
[[Category: thf-binding]] | [[Category: thf-binding]] | ||
[[Category: trna-modification]] | [[Category: trna-modification]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:56:58 2008'' |
Revision as of 21:56, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | TrmE (Thermotoga maritima) | ||||||
| Related: | 1XZQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 00:56:58 2008
