1wme

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(New page: 200px<br /><applet load="1wme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wme, resolution 1.50&Aring;" /> '''Crystal Structure of...)
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[[Image:1wme.gif|left|200px]]<br /><applet load="1wme" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wme, resolution 1.50&Aring;" />
 
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'''Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K)'''<br />
 
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==Overview==
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==Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K)==
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The crystal structure of an oxidatively stable subtilisin-like alkaline, serine protease, KP-43 from Bacillus sp. KSM-KP43, with a C-terminal, extension domain, was determined by the multiple isomorphous replacements, method with anomalous scattering. The native form was refined to a, crystallographic R factor of 0.134 (Rfree of 0.169) at 1.30-A resolution., KP-43 consists of two domains, a subtilisin-like alpha/beta domain and a, C-terminal jelly roll beta-barrel domain. The topological architecture of, the molecule is similar to that of kexin and furin, which belong to the, subtilisin-like proprotein convertases, whereas the amino acid sequence, and the binding orientation of the C-terminal beta-barrel domain both, differ in each case. Since the C-terminal domains of subtilisin-like, proprotein convertases are essential for folding themselves, the domain of, KP-43 is also thought to play such a role. KP-43 is known to be an, oxidation-resistant protease among the general subtilisin-like proteases., To investigate how KP-43 resists oxidizing reagents, the structure of, oxidized KP-43 was also determined and refined to a crystallographic R, factor of 0.142 (Rfree of 0.212) at 1.73-A resolution. The structure, analysis revealed that Met-256, adjacent to catalytic Ser-255, was, oxidized similarly to an equivalent residue in subtilisin BPN'. Although, KP-43, as well as proteinase K and subtilisin Carlsberg, lose their, hydrolyzing activity against synthetic peptides after oxidation treatment, all of them retain 70-80% activity against proteinaceous substrates. These, results, as well as the beta-casein digestion pattern analysis, have, indicated that the oxidation of the methionine adjacent to the catalytic, serine is not a dominant modification but might alter the substrate, specificities.
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<StructureSection load='1wme' size='340' side='right'caption='[[1wme]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1wme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._KSM-KP43 Bacillus sp. KSM-KP43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WME FirstGlance]. <br>
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1WME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WME OCA].
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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]] 1.5&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
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==Reference==
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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=1wme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wme OCA], [https://pdbe.org/1wme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wme RCSB], [https://www.ebi.ac.uk/pdbsum/1wme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wme ProSAT]</span></td></tr>
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The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal beta-barrel domain., Nonaka T, Fujihashi M, Kita A, Saeki K, Ito S, Horikoshi K, Miki K, J Biol Chem. 2004 Nov 5;279(45):47344-51. Epub 2004 Sep 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15342641 15342641]
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</table>
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[[Category: Bacteria]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/Q93UV9_9BACI Q93UV9_9BACI]
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[[Category: Fujihashi, M.]]
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== Evolutionary Conservation ==
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[[Category: Horikoshi, K.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Ito, S.]]
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Check<jmol>
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[[Category: Kita, A.]]
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<jmolCheckbox>
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[[Category: Miki, K.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/1wme_consurf.spt"</scriptWhenChecked>
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[[Category: Nonaka, T.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Saeki, K.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: CA]]
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</jmolCheckbox>
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[[Category: alpha-beta hydrolase fold]]
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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=1wme ConSurf].
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[[Category: jelly-roll beta-barrel]]
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<div style="clear:both"></div>
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__TOC__
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:15:16 2007''
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</StructureSection>
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[[Category: Bacillus sp. KSM-KP43]]
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[[Category: Large Structures]]
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[[Category: Fujihashi M]]
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[[Category: Horikoshi K]]
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[[Category: Ito S]]
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[[Category: Kita A]]
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[[Category: Miki K]]
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[[Category: Nonaka T]]
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[[Category: Saeki K]]

Current revision

Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K)

PDB ID 1wme

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