1xzp

<table><tr><td colspan='2'>[[1xzp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XZP FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xzq|1xzq]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TrmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xzp OCA], [http://pdbe.org/1xzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xzp RCSB], [http://www.ebi.ac.uk/pdbsum/1xzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xzp ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MNME_THEMA MNME_THEMA]] Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15616586</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1xzp" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Armengod, M E]]

[[Category: Scrima, A]]

[[Category: Vetter, I R]]

[[Category: Wittinghofer, A]]

[[Category: Gtp-binding]]

[[Category: Hydrolase]]

[[Category: Trna-modification]]