1s02

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[[Image:1s02.gif|left|200px]]
 
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{{Structure
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==EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN'==
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|PDB= 1s02 |SIZE=350|CAPTION= <scene name='initialview01'>1s02</scene>, resolution 1.9&Aring;
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<StructureSection load='1s02' size='340' side='right'caption='[[1s02]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1s02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S02 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1s02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s02 OCA], [https://pdbe.org/1s02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s02 RCSB], [https://www.ebi.ac.uk/pdbsum/1s02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s02 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s0/1s02_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1s02 ConSurf].
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<div style="clear:both"></div>
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'''EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN''''
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==See Also==
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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==Overview==
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<references/>
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Variants designed using PROTEUS have been produced in an attempt to engineer stabilizing salt bridges into subtilisin BPN'. All the mutants constructed by site-directed mutagenesis were secreted by Bacillus subtilis, except L75K. Q19E, expressed as a single variant and also in a double variant, Q19E/Q271E, appears to form a stabilizing salt bridge based on X-ray crystal structure determination and differential scanning calorimeter measurements. Although the double mutant was found to be less thermodynamically stable than the wild-type, it did exhibit an autolytic stability about two-fold greater under hydrophobic conditions. Four variants, A98K, S89E, V26R and L235R, were found to be nearly identical to wild-type in thermal stability, indicative of stable structures without evidence of salt bridge formation. Variants Q271E, V51K and T164R led to structures that resulted in varying degrees of thermodynamic and autolytic instability. A computer-modeling analysis of the PROTEUS predictions reveals that the low percentage of salt bridge formation is probably due to an overly simplistic electrostatic model, which does not account for the geometry of the pairwise interactions.
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__TOC__
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</StructureSection>
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==About this Structure==
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1S02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S02 OCA].
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==Reference==
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Effects of engineered salt bridges on the stability of subtilisin BPN'., Erwin CR, Barnett BL, Oliver JD, Sullivan JF, Protein Eng. 1990 Oct;4(1):87-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2127106 2127106]
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[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Subtilisin]]
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[[Category: Barnett BL]]
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[[Category: Barnett, B L.]]
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[[Category: Erwin CR]]
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[[Category: Erwin, C R.]]
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[[Category: Oliver JD]]
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[[Category: Oliver, J D.]]
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[[Category: Sullivan JF]]
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[[Category: Sullivan, J F.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:58:37 2008''
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Current revision

EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN'

PDB ID 1s02

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