1xzp

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[[Image:1xzp.gif|left|200px]]
[[Image:1xzp.gif|left|200px]]
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{{Structure
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|PDB= 1xzp |SIZE=350|CAPTION= <scene name='initialview01'>1xzp</scene>, resolution 2.3&Aring;
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|GENE= TrmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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{{STRUCTURE_1xzp| PDB=1xzp | SCENE= }}
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|RELATEDENTRY=[[1xzq|1XZQ]]
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|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>
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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.]]
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[[Category: gtp-binding]]
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[[Category: Gtp-binding]]
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[[Category: thf-binding]]
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[[Category: Thf-binding]]
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[[Category: trna-modification]]
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[[Category: Trna-modification]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:42:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:56:58 2008''
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Revision as of 12:42, 3 May 2008

Image:1xzp.gif

Template:STRUCTURE 1xzp

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

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