1ze2

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[[Image:1ze2.gif|left|200px]]
 
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{{Structure
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==Conformational change of pseudouridine 55 synthase upon its association with RNA substrate==
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|PDB= 1ze2 |SIZE=350|CAPTION= <scene name='initialview01'>1ze2</scene>, resolution 3.0&Aring;
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<StructureSection load='1ze2' size='340' side='right'caption='[[1ze2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=FHU:(5S,6R)-5-FLUORO-6-HYDROXY-PSEUDOURIDINE-5&#39;-MONOPHOSPHATE'>FHU</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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<table><tr><td colspan='2'>[[1ze2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZE2 FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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|GENE= truB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FHU:(5S,6R)-5-FLUORO-6-HYDROXY-PSEUDOURIDINE-5-MONOPHOSPHATE'>FHU</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ze2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ze2 OCA], [https://pdbe.org/1ze2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ze2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ze2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ze2 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ze1|1ZE1]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ze2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ze2 OCA], [http://www.ebi.ac.uk/pdbsum/1ze2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ze2 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/TRUB_THEMA TRUB_THEMA] Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/1ze2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ze2 ConSurf].
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<div style="clear:both"></div>
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'''Conformational change of pseudouridine 55 synthase upon its association with RNA substrate'''
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==See Also==
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*[[Guide-independent Pseudouridine synthase|Guide-independent Pseudouridine synthase]]
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*[[Pseudouridine synthase|Pseudouridine synthase]]
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==Overview==
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*[[Pseudouridine synthase 3D structures|Pseudouridine synthase 3D structures]]
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Pseudouridine 55 synthase (Psi55S) catalyzes isomerization of uridine (U) to pseudouridine (Psi) at position 55 in transfer RNA. The crystal structures of Thermotoga maritima Psi55S, and its complex with RNA, have been determined at 2.9 and 3.0 A resolutions, respectively. Structural comparisons with other families of pseudouridine synthases (PsiS) indicate that Psi55S may acquire its ability to recognize a stem-loop RNA substrate by two insertions of polypeptides into the PsiS core. The structure of apo-Psi55S reveals that these two insertions interact with each other. However, association with RNA substrate induces substantial conformational change in one of the insertions, resulting in disruption of interaction between insertions and association of both insertions with the RNA substrate. Specific interactions between two insertions, as well as between the insertions and the RNA substrate, account for the molecular basis of the conformational change.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1ZE2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZE2 OCA].
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==Reference==
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Conformational change of pseudouridine 55 synthase upon its association with RNA substrate., Phannachet K, Huang RH, Nucleic Acids Res. 2004 Feb 27;32(4):1422-9. Print 2004. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14990747 14990747]
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[[Category: Pseudouridylate synthase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Huang, R H.]]
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[[Category: Huang RH]]
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[[Category: Phannachet, K.]]
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[[Category: Phannachet K]]
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[[Category: protein-rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:40 2008''
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Current revision

Conformational change of pseudouridine 55 synthase upon its association with RNA substrate

PDB ID 1ze2

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