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New page: left|200px<br /><applet load="1wmd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wmd, resolution 1.30Å" /> '''Crystal Structure of...
 
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[[Image:1wmd.gif|left|200px]]<br /><applet load="1wmd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wmd, resolution 1.30&Aring;" />
'''Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)'''<br />


==Overview==
==Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)==
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.
<StructureSection load='1wmd' size='340' side='right'caption='[[1wmd]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1WMD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with CA, SO4, DIO and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WMD OCA].  
</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>
 
<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>
==Reference==
<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>
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]
</table>
[[Category: Bacteria]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/Q93UV9_9BACI Q93UV9_9BACI]  
[[Category: Fujihashi, M.]]
== Evolutionary Conservation ==
[[Category: Horikoshi, K.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Ito, S.]]
Check<jmol>
[[Category: Kita, A.]]
  <jmolCheckbox>
[[Category: Miki, K.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/1wmd_consurf.spt"</scriptWhenChecked>
[[Category: Nonaka, T.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Saeki, K.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: CA]]
  </jmolCheckbox>
[[Category: DIO]]
</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].
[[Category: GOL]]
<div style="clear:both"></div>
[[Category: SO4]]
__TOC__
[[Category: alpha-beta hydrolase fold]]
</StructureSection>
[[Category: jelly-roll beta-barrel]]
[[Category: Bacillus sp. KSM-KP43]]
 
[[Category: Large Structures]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:14:56 2007''
[[Category: Fujihashi M]]
[[Category: Horikoshi K]]
[[Category: Ito S]]
[[Category: Kita A]]
[[Category: Miki K]]
[[Category: Nonaka T]]
[[Category: Saeki K]]

Latest revision as of 13:32, 13 March 2024

Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)

1wmd, resolution 1.30Å

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