1hyf

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<StructureSection load='1hyf' size='340' side='right'caption='[[1hyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1hyf' size='340' side='right'caption='[[1hyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== 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/Aspoz Aspoz]. 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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<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='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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</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></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>
<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>
<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>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNT1_ASPOR RNT1_ASPOR]
== 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=1hyf 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=1hyf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:11453993<ref>PMID:11453993</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1hyf" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspoz]]
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[[Category: Aspergillus oryzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Langhorst, U]]
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[[Category: De Swarte J]]
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[[Category: Loris, R]]
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[[Category: De Vos S]]
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[[Category: Steyaert, J]]
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[[Category: Langhorst U]]
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[[Category: Swarte, J De]]
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[[Category: Loris R]]
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[[Category: Vos, S De]]
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[[Category: Steyaert J]]
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[[Category: Hydrolase]]
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[[Category: Metal binding]]
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[[Category: Ribonuclease]]
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[[Category: Stability]]
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Revision as of 07:42, 3 April 2024

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+

PDB ID 1hyf

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