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1au9

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SUBTILISIN BPN' MUTANT 8324 IN CITRATE

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Retrieved from "http://52.214.119.220/wiki/index.php/1au9"

Categories: Bacillus amyloliquefaciens | Large Structures | Howard AJ | Whitlow M | Wood JF

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-[[Image:1au9.gif|left|200px]]<br />
-<applet load="1au9" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1au9, resolution 1.80&Aring;" />
-'''SUBTILISIN BPN' MUTANT 8324 IN CITRATE'''<br />
-==Overview==
+==SUBTILISIN BPN' MUTANT 8324 IN CITRATE==
-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)]]
+<StructureSection load='1au9' size='340' side='right'caption='[[1au9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1au9]] 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=1AU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AU9 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]] 1.8&#8491;</td></tr>
+<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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=1au9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au9 OCA], [https://pdbe.org/1au9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1au9 RCSB], [https://www.ebi.ac.uk/pdbsum/1au9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1au9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/au/1au9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1au9 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-AU9 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, UNX and IPA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AU9 OCA]].
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
+== References ==
-==Reference==
+<references/>
-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]
+__TOC__
+</StructureSection>
 [[Category: Bacillus amyloliquefaciens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Howard, A.J.]]
+[[Category: Howard AJ]]
-[[Category: Whitlow, M.]]
+[[Category: Whitlow M]]
-[[Category: Wood, J.F.]]
+[[Category: Wood JF]]
-[[Category: CA]]
-[[Category: IPA]]
-[[Category: UNX]]
-[[Category: hydrolase]]
-[[Category: serine protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:05:27 2007''

1au9

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SUBTILISIN BPN' MUTANT 8324 IN CITRATE

Structural highlights

Function

Evolutionary Conservation

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