1si9

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[[Image:1si9.jpg|left|200px]]
 
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==Boiling stable protein isolated from Populus tremula==
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The line below this paragraph, containing "STRUCTURE_1si9", creates the "Structure Box" on the page.
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<StructureSection load='1si9' size='340' side='right'caption='[[1si9]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1si9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SI9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.27&#8491;</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=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1si9| PDB=1si9 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1si9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si9 OCA], [https://pdbe.org/1si9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1si9 RCSB], [https://www.ebi.ac.uk/pdbsum/1si9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1si9 ProSAT]</span></td></tr>
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</table>
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'''Boiling stable protein isolated from Populus tremula'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q9AR79_POPTN Q9AR79_POPTN]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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We previously reported on a new boiling stable protein isolated from aspen plants (Populus tremula), which we named SP1. SP1 is a stress-related protein with no significant sequence homology to other stress-related proteins. It is a 108-amino-acid hydrophilic polypeptide with a molecular mass of 12.4 kDa (Wang, W. X., Pelah, D., Alergand, T., Shoseyov, O., and Altman, A. (2002) Plant Physiol. 130, 865-875) and is found in an oligomeric form. Preliminary electron microscopy studies and matrix-assisted laser desorption ionization time-of-flight mass spectrometry experiments showed that SP1 is a dodecamer composed of two stacking hexamers. We performed a SDS-PAGE analysis, a differential scanning calorimetric study, and crystal structure determination to further characterize SP1. SDS-PAGE indicated a spontaneous assembly of SP1 to one stable oligomeric form, a dodecamer. Differential scanning calorimetric showed that SP1 has high thermostability i.e. Tm of 107 degrees C (at pH 7.8). The crystal structure of SP1 was initially determined to 2.4 A resolution by multi-wavelength anomalous dispersion method from a crystal belonging to the space group I422. The phases were extended to 1.8 A resolution using data from a different crystal form (P21). The final refined molecule includes 106 of the 108 residues and 132 water molecules (on average for each chain). The R-free is 20.1%. The crystal structure indicated that the SP1 molecule has a ferredoxin-like fold. Strong interactions between each two molecules create a stable dimer. Six dimers associate to form a ring-like-shaped dodecamer strongly resembling the particle visualized in the electron microscopy studies. No structural similarity was found between the crystal structure of SP1 and the crystal structure of other stress-related proteins such as small heat shock proteins, whose structure has been already determined. This structural study further supports our previous report that SP1 may represent a new family of stress-related proteins with high thermostability and oligomerization.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/si/1si9_consurf.spt"</scriptWhenChecked>
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1SI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SI9 OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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The structural basis of the thermostability of SP1, a novel plant (Populus tremula) boiling stable protein., Dgany O, Gonzalez A, Sofer O, Wang W, Zolotnitsky G, Wolf A, Shoham Y, Altman A, Wolf SG, Shoseyov O, Almog O, J Biol Chem. 2004 Dec 3;279(49):51516-23. Epub 2004 Sep 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15371455 15371455]
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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=1si9 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Populus tremula]]
[[Category: Populus tremula]]
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[[Category: Single protein]]
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[[Category: Almog O]]
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[[Category: Almog, O.]]
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[[Category: Dgany O]]
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[[Category: Dgany, O.]]
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[[Category: Gonzales A]]
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[[Category: Gonzales, A.]]
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[[Category: Shoseyov O]]
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[[Category: Shoseyov, O.]]
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[[Category: Sofer O]]
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[[Category: Sofer, O.]]
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[[Category: Wolf SG]]
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[[Category: Wolf, S G.]]
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[[Category: Boiling-soluble]]
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[[Category: Heat shock responsive]]
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[[Category: Stress]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:44:18 2008''
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Current revision

Boiling stable protein isolated from Populus tremula

PDB ID 1si9

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