2za4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structural Analysis of Barnase-barstar Complex== | ==Crystal Structural Analysis of Barnase-barstar Complex== | ||
<StructureSection load='2za4' size='340' side='right' caption='[[2za4]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='2za4' size='340' side='right' caption='[[2za4]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x1u|1x1u]], [[1x1w|1x1w]], [[1x1x|1x1x]], [[1x1y|1x1y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x1u|1x1u]], [[1x1w|1x1w]], [[1x1x|1x1x]], [[1x1y|1x1y]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2za4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za4 OCA], [http://pdbe.org/2za4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za4 RCSB], [http://www.ebi.ac.uk/pdbsum/2za4 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2za4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za4 OCA], [http://pdbe.org/2za4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za4 RCSB], [http://www.ebi.ac.uk/pdbsum/2za4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2za4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 13: | Line 14: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2za4_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2za4_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 42: | Line 43: | ||
[[Category: Ito, N]] | [[Category: Ito, N]] | ||
[[Category: Urakubo, Y]] | [[Category: Urakubo, Y]] | ||
[[Category: Cytoplasm]] | |||
[[Category: Endonuclease]] | [[Category: Endonuclease]] | ||
[[Category: Genetically modified food]] | |||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Revision as of 12:25, 17 October 2018
Crystal Structural Analysis of Barnase-barstar ComplexCrystal Structural Analysis of Barnase-barstar Complex
Structural highlights
Function[RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. [BARS_BACAM] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe complex of barnase (bn) and barstar (bs), which has been widely studied as a model for quantitative analysis of protein-protein interactions, is significantly destabilized by a single mutation, namely, bs Asp39 --> Ala, which corresponds to a change of 7.7 kcal x mol(-1) in the free energy of binding. However, there has been no structural information available to explain such a drastic destabilization. In the present study, we determined the structure of the mutant complex at 1.58 A resolution by X-ray crystallography. The complex was similar to the wild-type complex in terms of overall and interface structures; however, the hydrogen bond network mediated by water molecules at the interface was significantly different. Several water molecules filled the cavity created by the mutation and consequently caused rearrangement of the hydrated water molecules at the interface. The water molecules were redistributed into a channel-like structure that penetrated into the complex. Furthermore, molecular dynamics simulations showed that the mutation increased the mobility of water molecules at the interface. Since such a drastic change in hydration was not observed in other mutant complexes of bn and bs, the significant destabilization of the interaction may be due to this channel-like structure of hydrated water molecules. Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation.,Urakubo Y, Ikura T, Ito N Protein Sci. 2008 Jun;17(6):1055-65. Epub 2008 Apr 25. PMID:18441234[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||