2cj5
From Proteopedia
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| - | [[Image:2cj5.gif|left|200px]] | ||
| - | + | ==Crystal Structure of a Cell Wall Invertase Inhibitor from Tobacco (pH 5.0)== | |
| - | + | <StructureSection load='2cj5' size='340' side='right'caption='[[2cj5]], [[Resolution|resolution]] 1.84Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2cj5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJ5 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]] 1.84Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cj5 OCA], [https://pdbe.org/2cj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cj5 RCSB], [https://www.ebi.ac.uk/pdbsum/2cj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cj5 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/O49908_TOBAC O49908_TOBAC] | |
| - | + | == 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/cj/2cj5_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=2cj5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Plant acid invertases catalyse the breakdown of sucrose. Their activity is tightly regulated through interaction with specific protein inhibitors. The complex between the cell-wall invertase inhibitor Nt-CIF and its target enzyme is stable only at acidic pH, as found in the plant cell wall. Since the pH in this compartment can be modulated between pH 4 and 6 in planta, the rapid dissociation of the inhibitor-enzyme complex at neutral pH may represent a regulatory event. Here, it is analyzed whether the inhibitory component undergoes structural rearrangements upon changes in the pH environment. Six crystal forms grown at pH 4.6-9.5 and diffracting up to 1.63 Angstrom indicate only small structural changes in CIF. This suggests that complex dissociation at neutral pH is mediated either by rearrangements in the enzyme or by a complex pattern of surface charges in the inhibitor-enzyme binding interface. | Plant acid invertases catalyse the breakdown of sucrose. Their activity is tightly regulated through interaction with specific protein inhibitors. The complex between the cell-wall invertase inhibitor Nt-CIF and its target enzyme is stable only at acidic pH, as found in the plant cell wall. Since the pH in this compartment can be modulated between pH 4 and 6 in planta, the rapid dissociation of the inhibitor-enzyme complex at neutral pH may represent a regulatory event. Here, it is analyzed whether the inhibitory component undergoes structural rearrangements upon changes in the pH environment. Six crystal forms grown at pH 4.6-9.5 and diffracting up to 1.63 Angstrom indicate only small structural changes in CIF. This suggests that complex dissociation at neutral pH is mediated either by rearrangements in the enzyme or by a complex pattern of surface charges in the inhibitor-enzyme binding interface. | ||
| - | + | Multiple crystal forms of the cell-wall invertase inhibitor from tobacco support high conformational rigidity over a broad pH range.,Hothorn M, Scheffzek K Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):665-70. Epub 2006, May 12. PMID:16699194<ref>PMID:16699194</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2cj5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Nicotiana tabacum]] | [[Category: Nicotiana tabacum]] | ||
| - | + | [[Category: Hothorn M]] | |
| - | [[Category: Hothorn | + | [[Category: Scheffzek K]] |
| - | [[Category: Scheffzek | + | |
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Current revision
Crystal Structure of a Cell Wall Invertase Inhibitor from Tobacco (pH 5.0)
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