1a2q

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[[Image:1a2q.gif|left|200px]]<br />
 
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<applet load="1a2q" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a2q, resolution 1.80&Aring;" />
 
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'''SUBTILISIN BPN' MUTANT 7186'''<br />
 
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==Overview==
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==SUBTILISIN BPN' MUTANT 7186==
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Six individual amino acid substitutions at separate positions in the, tertiary structure of subtilisin BPN' (EC 3.4.21.14) were found to, increase the stability of this enzyme, as judged by differential scanning, calorimetry and decreased rates of thermal inactivation. These stabilizing, changes, N218S, G169A, Y217K, M50F, Q206C, and N76D, were discovered, through the use of five different investigative approaches: (1) random, mutagenesis; (2) design of buried hydrophobic side groups; (3) design of, electrostatic interactions at Ca2+ binding sites; (4) sequence homology, consensus; and (5) serendipity. Individually, the six amino acid, substitutions increase the delta G of unfolding between 0.3 and 1.3, kcal/mol at 58.5 degrees C. The combination of these six individual, stabilizing ... [[http://ispc.weizmann.ac.il/pmbin/getpm?2684274 (full description)]]
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<StructureSection load='1a2q' size='340' side='right'caption='[[1a2q]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1a2q]] 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=1A2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2Q FirstGlance]. <br>
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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]] 1.8&#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=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MIS:MONOISOPROPYLPHOSPHORYLSERINE'>MIS</scene></td></tr>
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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=1a2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2q OCA], [https://pdbe.org/1a2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2q RCSB], [https://www.ebi.ac.uk/pdbsum/1a2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2q 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/a2/1a2q_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=1a2q ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1A2Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]] with CA and ACN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: 169, 218, C22, C87, CA1 and CA2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A2Q OCA]].
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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==Reference==
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<references/>
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Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2684274 2684274]
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__TOC__
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</StructureSection>
[[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: Gilliland GL]]
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[[Category: Gilliland, G.L.]]
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[[Category: Howard AJ]]
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[[Category: Howard, A.J.]]
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[[Category: Whitlow M]]
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[[Category: Whitlow, M.]]
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[[Category: ACN]]
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[[Category: CA]]
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[[Category: hydrolase]]
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[[Category: serine protease]]
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[[Category: sporulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:44:16 2007''
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Current revision

SUBTILISIN BPN' MUTANT 7186

PDB ID 1a2q

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