1r3f

<StructureSection load='1r3f' size='340' side='right' caption='[[1r3f]], [[Resolution|resolution]] 1.85&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R3F FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r3e|1r3e]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRUB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3f OCA], [http://pdbe.org/1r3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r3f RCSB], [http://www.ebi.ac.uk/pdbsum/1r3f PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/TRUB_ECOLI TRUB_ECOLI]] Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.<ref>PMID:7489483</ref> <ref>PMID:11142385</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r3/1r3f_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

RNA pseudouridine synthase, TruB, catalyzes pseudouridine formation at U55 in tRNA. This posttranscriptional modification is almost universally conserved and occurs in the T arm of most tRNAs. We determined the crystal structure of Escherichia coli TruB apo enzyme, as well as the structure of Thermotoga maritima TruB in complex with RNA. Comparison of the RNA-free and -bound forms of TruB reveals that this enzyme undergoes significant conformational changes on binding to its substrate. These conformational changes include the ordering of the "thumb loop," which binds right into the RNA hairpin loop, and a 10 degree hinge movement of the C-terminal domain. Along with the result of docking experiments performed on apo TruB, we conclude that TruB recognizes its RNA substrate through a combination of rigid docking and induced fit, with TruB first rigidly binding to its target and then maximizing the interaction by induced fit.

Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit.,Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12648-53. Epub 2003 Oct 17. PMID:14566049<ref>PMID:14566049</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 1r3f" style="background-color:#fffaf0;"></div>

*[[TRNA pseudouridine synthase|TRNA pseudouridine synthase]]

[[Category: Bacillus coli migula 1895]]

[[Category: Pseudouridylate synthase]]

[[Category: Agarwalla, S]]

[[Category: Finer-Moore, J]]

[[Category: Moustakas, D T]]

[[Category: Pan, H]]

[[Category: Stroud, R M]]

[[Category: Rna modification]]