1i0x: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1i0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i0x, resolution 1.65Å" /> '''RIBONUCLEASE T1 IN C... |
No edit summary |
||
| (19 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)== | ||
In the crystalline state, ribonuclease T1 binds calcium ions at different | <StructureSection load='1i0x' size='340' side='right'caption='[[1i0x]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1i0x]] is a 4 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=1I0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I0X FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</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=CA:CALCIUM+ION'>CA</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=1i0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i0x OCA], [https://pdbe.org/1i0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i0x RCSB], [https://www.ebi.ac.uk/pdbsum/1i0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i0x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNT1_ASPOR RNT1_ASPOR] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i0/1i0x_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1i0x ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1i0x" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: De Swarte J]] | ||
[[Category: De Vos S]] | |||
[[Category: Langhorst U]] | |||
[[Category: Loris R]] | |||
[[Category: | [[Category: Steyaert J]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 03:04, 21 November 2024
RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)RIBONUCLEASE T1 IN COMPLEX WITH 2'GMP (FORM II CRYSTAL)
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 |
| ||||||||||||||||||