1si7: Difference between revisions

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<StructureSection load='1si7' size='340' side='right'caption='[[1si7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1si7' size='340' side='right'caption='[[1si7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1si7]] 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=1SI7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SI7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1si7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SI7 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRUD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=1si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si7 OCA], [https://pdbe.org/1si7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1si7 RCSB], [https://www.ebi.ac.uk/pdbsum/1si7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1si7 ProSAT]</span></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=1si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si7 OCA], [http://pdbe.org/1si7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1si7 RCSB], [http://www.ebi.ac.uk/pdbsum/1si7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1si7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRUD_ECOLI TRUD_ECOLI]] Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.<ref>PMID:12756329</ref>
[https://www.uniprot.org/uniprot/TRUD_ECOLI TRUD_ECOLI] Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.<ref>PMID:12756329</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1si7 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1si7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel alpha/beta fold that up to now has not been found in any other protein.
Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold.,Kaya Y, Del Campo M, Ofengand J, Malhotra A J Biol Chem. 2004 Apr 30;279(18):18107-10. Epub 2004 Mar 3. PMID:14999002<ref>PMID:14999002</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1si7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pseudouridylate synthase]]
[[Category: Del Campo M]]
[[Category: Campo, M Del]]
[[Category: Kaya Y]]
[[Category: Kaya, Y]]
[[Category: Malhotra A]]
[[Category: Malhotra, A]]
[[Category: Ofengand J]]
[[Category: Ofengand, J]]
[[Category: Lyase]]
[[Category: Novel fold]]
[[Category: Pseudouridine synthase]]
[[Category: Trna]]
[[Category: Trud]]

Latest revision as of 08:30, 14 February 2024

Structure of E. coli tRNA psi 13 pseudouridine synthase TruD

1si7, resolution 2.20Å

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