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1hyf

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(New page: 200px<br /><applet load="1hyf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyf, resolution 1.70&Aring;" /> '''RIBONUCLEASE T1 V16A...)
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[[Image:1hyf.gif|left|200px]]<br /><applet load="1hyf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hyf, resolution 1.70&Aring;" />
 
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'''RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+'''<br />
 
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==Overview==
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==RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+==
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In the crystalline state, ribonuclease T1 binds calcium ions at different, lattice-dependent positions. In solution, its conformational stability is, also remarkably increased in the presence of divalent metal ions., Combining urea unfolding studies and X-ray crystallography, we compared, the presence of several metal ions at specific sites in the protein to, their contribution to the overall stabilizing effect in solution. We, constructed thermodynamic cycles involving particular metal ions and, specific carboxylate functions. The resulting coupling energies indicate, that some (but not all) metal ions found at lattice contacts in crystal, structures may indeed significantly contribute to stability enhancement in, the presence of metal ions in solution.
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<StructureSection load='1hyf' size='340' side='right'caption='[[1hyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hyf]] is a 1 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=1HYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYF 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]] 1.7&#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=SR:STRONTIUM+ION'>SR</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=1hyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyf OCA], [https://pdbe.org/1hyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyf RCSB], [https://www.ebi.ac.uk/pdbsum/1hyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyf 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/hy/1hyf_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=1hyf 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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1HYF 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 SR 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=1HYF 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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The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution., Deswarte J, De Vos S, Langhorst U, Steyaert J, Loris R, Eur J Biochem. 2001 Jul;268(14):3993-4000. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11453993 11453993]
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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: De Swarte J]]
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[[Category: Langhorst, U.]]
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[[Category: De Vos S]]
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[[Category: Loris, R.]]
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[[Category: Langhorst U]]
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[[Category: Steyaert, J.]]
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[[Category: Loris R]]
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[[Category: Swarte, J.De.]]
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[[Category: Steyaert J]]
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[[Category: Vos, S.De.]]
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[[Category: 2GP]]
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[[Category: SR]]
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[[Category: metal binding]]
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[[Category: ribonuclease]]
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[[Category: stability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:54:35 2007''
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Current revision

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+

PDB ID 1hyf

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