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1trp

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(New page: 200px<br /><applet load="1trp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1trp, resolution 2.4&Aring;" /> '''X-RAY CRYSTALLOGRAPHI...)
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[[Image:1trp.gif|left|200px]]<br /><applet load="1trp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1trp, resolution 2.4&Aring;" />
 
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'''X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1'''<br />
 
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==Overview==
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==X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1==
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Two mutants of ribonuclease T1 (RNaseT1), [59-tyrosine]ribonuclease T1, (W59Y) and [45-tryptophan,59-tyrosine]ribonuclease T1 (Y45W/W59Y) possess, between 150% and 190% wild-type activity. They have been crystallised as, complexes of the inhibitor 2'-guanylic acid and analysed by X-ray, diffraction at resolutions of 0.23 nm and 0.24 nm, respectively. The space, group for both is monoclinic, P2(1), with two molecules/asymmetric unit, W59Y: a = 4.934 nm, b = 4.820 nm, c = 4.025 nm, beta = 90.29 degrees., Y45W/W59Y: a = 4.915 nm, b = 4.815 nm, c = 4.015 nm, beta = 90.35 degrees., Compared to wild-type RNaseT1 in complex with 2'-guanylic acid (2'GMP), both mutant inhibitor complexes indicate that the replacement of Trp59 by, Tyr leads to a 0.04-nm inward shift of the single alpha-helix and to, significant differences in the active-site geometry, inhibitor, conformation and inhibitor binding. Calorimetric studies of a range of, mutants [24-tryptophan]ribonuclease T1 (Y24W), [42-tryptophan]ribonuclease, T1 (Y42W), [45-tryptophan]ribonuclease T1 (Y45W), [92-alanine]ribonuclease, T1 (H92A) and [92-threonine]ribonuclease T1 (H92T) with and without the, further mutation Trp59--&gt;Tyr showed that mutant proteins for which Trp59, is replaced by Tyr exhibit slightly decreased thermal stability.
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<StructureSection load='1trp' size='340' side='right'caption='[[1trp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1trp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRP FirstGlance]. <br>
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2GP:GUANOSINE-2-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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=1trp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1trp OCA], [https://pdbe.org/1trp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1trp RCSB], [https://www.ebi.ac.uk/pdbsum/1trp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1trp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNT1_ASPOR RNT1_ASPOR]
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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/tr/1trp_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=1trp ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TRP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA and 2GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TRP OCA].
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59--&gt;Tyr in ribonuclease T1., Schubert WD, Schluckebier G, Backmann J, Granzin J, Kisker C, Choe HW, Hahn U, Pfeil W, Saenger W, Eur J Biochem. 1994 Mar 1;220(2):527-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8125111 8125111]
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[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
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[[Category: Ribonuclease T(1)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Saenger W]]
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[[Category: Saenger, W.]]
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[[Category: Schluckebier G]]
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[[Category: Schluckebier, G.]]
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[[Category: 2GP]]
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[[Category: CA]]
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[[Category: hydrolase(endoribonuclease)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:32:39 2007''
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Current revision

X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1

PDB ID 1trp

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