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==RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+== | ==RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+== | ||
<StructureSection load='1hz1' size='340' side='right' caption='[[1hz1]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1hz1' size='340' side='right'caption='[[1hz1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hz1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1hz1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZ1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hz1 OCA], [https://pdbe.org/1hz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hz1 RCSB], [https://www.ebi.ac.uk/pdbsum/1hz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hz1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[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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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hz1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hz1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 29: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[ | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspergillus niger]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: De Swarte J]] | ||
[[Category: De Vos S]] | |||
[[Category: | [[Category: Langhorst U]] | ||
[[Category: Loris R]] | |||
[[Category: | [[Category: Steyaert J]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 09:43, 30 October 2024
RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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