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[[Image:1wmd.gif|left|200px]]


{{Structure
==Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)==
|PDB= 1wmd |SIZE=350|CAPTION= <scene name='initialview01'>1wmd</scene>, resolution 1.30&Aring;
<StructureSection load='1wmd' size='340' side='right'caption='[[1wmd]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1wmd]] 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=1WMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WMD FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
|GENE=  
<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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmd OCA], [https://pdbe.org/1wmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wmd RCSB], [https://www.ebi.ac.uk/pdbsum/1wmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wmd ProSAT]</span></td></tr>
|RELATEDENTRY=[[1wme|1WME]], [[1wmf|1WMF]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmd OCA], [http://www.ebi.ac.uk/pdbsum/1wmd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wmd RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/Q93UV9_9BACI Q93UV9_9BACI]
 
== Evolutionary Conservation ==
'''Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/1wmd_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1WMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMD OCA].  
</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=1wmd ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
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://www.ncbi.nlm.nih.gov/pubmed/15342641 15342641]
</StructureSection>
[[Category: Bacteria]]
[[Category: Bacillus sp. KSM-KP43]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fujihashi, M.]]
[[Category: Fujihashi M]]
[[Category: Horikoshi, K.]]
[[Category: Horikoshi K]]
[[Category: Ito, S.]]
[[Category: Ito S]]
[[Category: Kita, A.]]
[[Category: Kita A]]
[[Category: Miki, K.]]
[[Category: Miki K]]
[[Category: Nonaka, T.]]
[[Category: Nonaka T]]
[[Category: Saeki, K.]]
[[Category: Saeki K]]
[[Category: alpha-beta hydrolase fold]]
[[Category: jelly-roll beta-barrel]]
 
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Retrieved from "https://proteopedia.org/1wmd"